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Petri Kursula

Professor, Biochemistry and Molecular Biology

Our main focus is the structural biology of the myelin sheath. Most myelin proteins are either integral or peripheral membrane proteins, often involved in either autoimmune or inherited demyelinating neurological diseases. For some more details, please see my research project home page. We also have a keen interest in other structural biology problems, including protein-membrane interactions at the molecular level and the structural basis of various neurological diseases.

2017

Ponna S.K., Myllykoski M., Boeckers T.M. & Kursula P. (2017) Structure of an unconventional SH3 domain from the postsynaptic density protein Shank3 at ultrahigh resolution. Biochem. Biophys. Res. Commun., in press

Ruskamo S., Nieminen T., Kristiansen C.K., Vatne G.H., Baumann A., Hallin E.I., Raasakka A., Joensuu P., Bergmann U., Vattulainen I. & Kursula P. (2017) Molecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2. Sci. Rep., in press.

Raasakka A., Ruskamo S., Kowal J., Barker R., Baumann A., Martel A., Tuusa J., Myllykoski M., Bürck J., Ulrich A.S., Stahlberg H. & Kursula P. (2017) Membrane association landscape of myelin basic protein portrays formation of the myelin major dense line. Sci. Rep., in press. 

Muruganandam G., Raasakka A., Myllykoski M., Kursula I. & Kursula P. (2017) Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase. BMC Biochem. 18:7.

Baumann A. & Kursula P. (2017) SUMO on CRMPs - wrestling for pain? Channels 24:1-3.

Han H. & Kursula P. (2017) Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin. Data Brief 11:552-556.

Tuusa J., Raasakka A., Ruskamo S. & Kursula P. (2017) Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments. Mult. Scler. Demyelinating Disord. 2:4.

Piirainen H., Taura J., Kursula P., Ciruela F. & Jaakola V.-P. (2017) Calcium modulates calmodulin/α-actinin 1 interaction with and agonist-dependent internalization of the adenosine A2A receptor. BBA Mol. Cell Res. 1864:674-686. 

Koski K., Anantharajan J., Kursula P., Dhavala P., Murthy A.V., Bergmann U., Myllyharju J. & Wierenga R.K. (2017) Assembly of the elongated collagen prolyl 4-hydroxylase α2β2 heterotetramer around a central α2 dimer. Biochem. J. 474:751-769.

Snaidero N., Velte C., Myllykoski M., Raasakka A., Ignatev A., Werner H.B., Erwig M.S., Möbius W., Kursula P., Nave K.A. & Simons M. (2017) Antagonistic functions of MBP and CNP establish cytosolic channels in CNS myelin. Cell Rep. 18:314-323. 

Myllykoski M. & Kursula P. (2017) Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase. PLoS ONE 12:e0170355. 

Myllykoski M., Baumann A., Hensley K. & Kursula P. (2017) Collapsin response mediator protein 2: high-resolution crystal structure sheds light on small-molecule binding, post-translational modifications, and conformational flexibility. Amino Acids 49:747-759. 

2016

Bezem M.T., Baumann A., Skjærven L., Meyer R., Kursula P., Martinez A., Flydal M.I. (2016) Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme. Sci. Rep. 6:30390.

Ponna S.K., Myllykoski M., Boeckers T.M. & Kursula P. (2016) Sub-atomic resolution X-ray diffraction of the SH3 domain from the post-synaptic density protein Shank3. bioRxiv; DOI: http://dx.doi.org/10.1101/051425.

Kouznetsova E., Kanno T., Karlberg T., Thorsell A.-G., Wisniewska M., Kursula P., Sjögren C. & Schüler H. (2016) Sister chromatic cohesion establishment factor ESCO1 operates by substrate-assisted catalysis. Structure 24:789-796.

Hensley K. & Kursula P. (2016) Collapsin response mediator protein-2 (CRMP2) is a plausible etiological factor and potential therapeutic target in Alzheimer’s disease: Comparison and contrast with microtubule-associated protein tau. J. Alzheimers Dis. 53:1-14.

Simon B., Huart A.-S., Temmerman K., Vahokoski J., Mertens H.D.T., Komadina D., Hoffmann J.-E., Yumerefendi H., Svergun D.I., Kursula P., Schultz C., McCarthy A.A., Hart D.J. & Wilmanns M. (2016) Death-associated protein kinase activity is regulated by coupled calcium/calmodulin binding to two distinct sites. Structure 24:851-861.

Myllykoski M., Seidel L., Muruganandam G., Raasakka A., Torda A.E. & Kursula P. (2016) Structural and functional evolution of 2´,3´-cyclic nucleotide 3´-phosphodiesterase. Brain Res. 1641: 64-78.

2015

Raasakka A., Myllykoski M., Laulumaa S., Lehtimäki M., Härtlein M., Moulin M., Kursula I. & Kursula P. (2015) Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase. Sci. Rep. 5:16520. 

Laulumaa S., Blakeley M.P., Raasakka A., Moulin M., Härtlein M. & Kursula P. (2015) Production, crystallization, and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2. Acta Cryst. F 71:1391-1395.

Bhargav S.P., Vahokoski J., Kallio J.P., Torda A., Kursula P. & Kursula I. (2015) Two independently folding units of Plasmodium profilin suggest evolution via gene fusion. Cell. Mol. Life Sci. 72:4193-4203. 

Laulumaa S., Nieminen T., Lehtimäki M., Aggarwal S., Simons M., Koza M.M., Vattulainen I., Kursula P. & Natali F. (2015) Dynamics of the peripheral membrane protein P2 from human myelin measured by neutron scattering - a comparison between wild-type protein and a hinge mutant. PLoS ONE 10:e0128954.

Chukhlieb M., Raasakka A., Ruskamo S. & Kursula P. (2015) The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. Amino Acids 47:1567-1577.

Freischmidt A., Wieland T., Richter B., Ruf W., Schaeffer V., Müller K., Marroquin N., Nordin F., Hübers A., Weydt P., Pinto S., Press R., Millecamps S., Molko N., Bernard E., Desnuelle C., Soriani M.-H., Dorst J., Graf E., Nordström U., Feiler M.S., Putz S., Böckers T.M., Meyer T., Winkler A.S., Winkelman J., de Carvalho M., Thal D.R., Otto M., Brännström T., Volk A.E., Kursula P., Danzer K.M., Lichtner P., Dikic I., Meitinger T., Ludolph A.C., Strom T.M., Andersen P.M. & Weishaupt J.H. (2015) Haploinsufficiency of TBK1 causes familial amyotrophic lateral sclerosis and fronto-temporal dementia. Nature Neurosci. 18: 631-636.

Piirainen H., Hellman M., Tossavainen H., Permi P., Kursula P. & Jaakola V.-P. (2015) Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. Biophys. J. 108: 903-917.

Laulumaa S., Kursula P. & Natali F. (2015) Neutron scattering studies on protein dynamics using the human myelin membrane protein P2. Eur. Phys. J. Web of Conferences 83: 02010.

Han H. & Kursula P. (2015) The olfactomedin domain from gliomedin is a beta-propeller with unique structural properties. J. Biol. Chem. 290: 3612-3621.

Onwukwe G.U., Kursula P., Koski M.K., Schmitz W. & Wierenga R.K. (2015) Human Δ3, Δ2-enoyl-CoA isomerase, type-2: a structural enzymology study on the catalytic role of its ACBP-domain and helix-10. FEBS J. 282: 746-768.

2014

Knoll W., Peters J., Kursula P., Gerelli Y. & Natali F. (2014) Influence of myelin proteins on the structure and dynamics of a model membrane with emphasis on the low temperature regime. J. Chem. Phys. 141: 205101. 

Han H. & Kursula P. (2014) Expression, purification, crystallization, and preliminary X-ray crystallographic analysis of the extracellular olfactomedin domain from gliomedin. Acta Cryst. F 70: 1536-1539. 

Kursula P. (2014) The many structural faces of calmodulin - a multitasking molecular jackknife. Amino Acids 46: 2295-2304.


Zenker J., Stettner M., Ruskamo S., Domènech-Estévez E., Baloui H., Médard J.-J., Verheijen M.H.G., Brouwers J.F., Kursula P., Kieseier B.C. & Chrast R. (2014) A role of peripheral myelin protein 2 in lipid homeostasis of myelinating Schwann cells. Glia 62: 1502-1512. 


Han H. & Kursula P. (2014) Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping. J. Biol. Chem. 289: 14121-14131.


Raasakka A. & Kursula P. (2014) The myelin membrane-associated enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase: on a highway to structure and function. Neurosci. Bull. 30: 956-966.


Kursula P. (2014) Crystallographic snapshots of initial steps in the collapse of the calmodulin central helix. Acta Cryst. D 70: 24-30.


Ruskamo S., Yadav R.P., Sharma S., Lehtimäki M., Laulumaa S., Aggarwal S., Simons M., Bürck J., Ulrich A.S., Juffer A.H., Kursula I. & Kursula P. (2014) Atomic-resolution view into structure-function relationships of the human myelin peripheral membrane protein P2. Acta Cryst. D 70: 165-176.


Szambowska A., Tessmer I., Kursula P., Usskilat C., Prus P., Pospiech H. & Grosse F. (2014) DNA binding properties of human Cdc45 suggest a function as a molecular wedge for DNA unwinding. Nucleic Acids Res. 42: 2308-2319.


Knoll W., Peters J., Kursula P., Gerelli Y., Ollivier J., Demé B., Telling M., Kemner E. & Natali F. (2014) Structural and dynamical properties of reconstituted myelin sheaths by myelin proteins MBP and P2 studied by neutron scattering. Soft Matter 10: 519-529.

2013

Muruganandam G., Bürck J., Ulrich A.S., Kursula I. & Kursula P. (2013) Lipid membrane association of myelin proteins and peptide segments studied by oriented and synchrotron radiation circular dichroism spectroscopy. J. Phys. Chem. B 117: 14983-14993.


Anantharajan J., Koski M.K., Kursula P., Hieta R., Bergmann U., Myllyharju J. & Wierenga R.K. (2013) The unique structural motifs for substrate binding and dimerisation of the alpha subunit of collagen prolyl 4-hydroxylase. Structure 12: 2107-2118.


Myllykoski M., Raasakka A., Lehtimäki M., Han H., Kursula I. & Kursula P. (2013) Crystallographic analysis of the reaction cycle of 2’,3’-cyclic nucleotide 3’-phosphodiesterase, a unique member of the 2H phosphoesterase family. J. Mol. Biol. 425: 4307-4322.


Han H. & Kursula P. (2013) Preliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, and abundant peripheral nerve protein linked to human neuropathies. Acta Cryst. F 69: 804-808.


Knoll W., Peters J., Gerelli Y., Kursula P. & Natali F. (2013) The influence of the myelin basic protein C8 mutant on the dynamics of myelin membranes. J. Phys. Soc. Jpn. 82: SA018.


Forst A.H., Karlberg T., Herzog N., Thorsell A.-G., Gross A., Feijs K.L., Verheugd P., Kursula P., Nijmeijer B., Kremmer E., Kleine H., Ladurner A., Schüler H. & Lüscher B. (2013) Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains. Structure 21: 462-475.


Han H., Myllykoski M., Ruskamo S., Wang C. & Kursula P. (2013) Myelin-specific proteins: a structurally diverse group of membrane-binding molecules. BioFactors 39: 233-241.

2012

Ruskamo S., Chukhlieb M., Vahokoski J., Bhargav S.P., Liang F., Kursula I. & Kursula P. (2012) Juxtanodin is an intrinsically disordered F-actin binding protein. Sci. Rep. 2: 899.


Lehtimäki M., Laulumaa S., Ruskamo S. & Kursula P. (2012) Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2. Acta Cryst. F 68: 1359-1362.


Myllykoski M., Itoh K., Kangas S.M., Heape A.M., Kang S.-U., Lubec G., Kursula I. & Kursula P. (2012) The N-terminal domain of the myelin enzyme 2’,3’-cyclic nucleotide 3’-phosphodiesterase: Direct molecular interaction with the calcium sensor calmodulin. J. Neurochem. 123: 515-524. 


Ignatev A., Bhargav S.P., Vahokoski J., Kursula P. & Kursula I. (2012) The lasso segment is required for functional dimerization of the Plasmodium formin 1 FH2 domain. PLoS ONE, 7: e33586.


Myllykoski M., Raasakka A., Han H. & Kursula P. (2012) Myelin 2’,3’-cyclic nucleotide 3’-phosphodiesterase: Active-site ligand binding and molecular conformation. PLoS ONE, 7: e32336.  


Chen W.-Q., Heymann G., Kursula P., Rosner M., Hengstschläger M., Huppertz H. & Lubec G. (2012) The effects of gigapascal level pressure on protein structure and function. J. Phys. Chem. B, 116: 1100-1110. 


Kuczera J. & Kursula P. (2012) Interactions of calmodulin with death-associated protein kinase peptides: experimental and modeling studies. J. Biomol. Struct. Dyn. 30: 45-61.


Myllykoski M., Baumgärtel P. & Kursula P. (2012) Conformations of peptides derived from myelin-specific proteins in membrane-mimetic conditions probed by synchrotron radiation CD spectroscopy. Amino Acids, 42: 1467-1474.


2011

Patton G.C., Stenmark P., Gollapalli D.R., Sevastik R., Kursula P., Flodin S., Schüler H., Swales C.T., Eklund H., Himo F., Nordlund P. & Hedstrom L. (2011) Cofactor mobility determines reaction outcome in the IMPDH amd GMPR (β-α)8 barrel enzymes. Nature Chem. Biol. 7: 950-958.


Wang C., Neugebauer U., Bürck J., Myllykoski M., Baumgärtel P., Popp J. & Kursula P. (2011) Charge isomers of myelin basic protein: Structure and interactions with membranes, nucleotide analogues, and calmodulin. PLoS ONE 6: e19915.


Patel A.K., Yadav R.P., Majava V., Kursula I. & Kursula P. (2011) Structure of the dimeric autoinhibited conformation of DAPK2, a pro-apoptotic protein kinase. J. Mol. Biol. 409: 369-383.


Patel A.K., Singh V.K., Bergmann U., Jagannadham M.V. & Kursula P. (2011) Purification, crystallization, and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex. Acta Cryst. F 67: 608-612.


Fukao T., Sass J.O., Kursula P., Thimm E., Wendel U., Ficicioglu C., Monastiri K., Guffon N., Baric I., Zabot M.T. & Kondo N. (2011) Clinical and molecular characterization of five patients with succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency. Biochim. Biophys. Acta 1812: 619-624.


2010

Wang C., Myllykoski M. & Kursula P. (2010) Biophysical studies on the structure and function of proteins from the vertebrate myelin sheath. Proc. SPIE 7376: 73760V.


Fukao T., Ishii T., Amano N., Kursula P., Takayanagi M., Murase K., Sakaguchi N., Kondo N. & Hasegawa T. (2010) A neonatal onset succinyl-CoA:3-ketoacid CoA transferase (SCOT)-deficient patient with T435N and c.658-666dupAACGTGATT p.N220_I222dup mutations in the OXCT1 gene. J. Inherit. Metab. Dis., in press.


Suresh S., Wang C., Nanekar R., Kursula P. & Edwardson J.M. (2010) Myelin basic protein and myelin protein 2 act synergistically to cause stacking of lipid bilayers. Biochemistry 49: 3456-3463.


Majava V., Polverini E., Mazzini A., Nanekar R., Knoll W., Peters J., Natali F., Baumgärtel P., Kursula I. & Kursula P. (2010) Structural and functional characterization of human peripheral nervous system myelin protein P2. PLoS ONE 5: e10300.


Chen W.-Q., Salmazo A., Myllykoski M., Sjöblom B., Bidlingmaier M., Pollak A., Baumgärtel P., Djinovic-Carugo K., Kursula P. & Lubec G. (2010) Purification of recombinant growth hormone by clear native gels for conformational analyses - Preservation of conformation and receptor binding.Amino Acids 39: 859-869.


Knoll W., Natali F., Peters J., Nanekar R., Wang C. & Kursula P. (2010) Dynamic properties of a reconstituted myelin sheath. Spectroscopy 24: 585-592.


de Diego I., Kuper J., Bakalova N., Kursula P. & Wilmanns M. (2010) Molecular basis of the death associated protein kinase-calcium/calmodulin regulator complex. Science Signaling 3:ra6.


Myllykoski M. & Kursula P. (2010) Expression, purification, and initial characterization of different domains of recombinant mouse 2',3'-cyclic nucleotide 3'-phosphodiesterase, an enigmatic enzyme from the myelin sheath. BMC Res. Notes 3:12.


Majava V., Wang C., Myllykoski M., Kangas S.M., Kang S.U., Hayashi N., Baumgärtel P., Heape A.M., Lubec G. & Kursula P. (2010) Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. Amino Acids 39:59-71.


Kursula P. (2010) Structural biology insights into the autoantigens of the myelin sheath. In Autoimmune Diseases: Symptoms, Diagnosis and Treatment, Nova Publishers.


2009

Meriläinen G., Poikela V., Kursula P. & Wierenga R. (2009) The thiolase reaction mechanism: the importance of Asn316 and His348 for stabilizing the enolate intermediate of the Claisen condensation. Biochemistry 48: 11011-11025.


Myllykoski M., Kuczera K. & Kursula P. (2009) Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: molecular conformation and energetics of binding. Biophys. Chem. 144: 130-135.


Behnen M., Murk K., Kursula P., Cappallo-Obermann H., Rothkegel M., Kierszenbaum A. & Kirchhoff C. (2009) Testis-expressed profilins 3 and 4 show distinct functional characteristics and localize in acroplaxome-manchette complex in spermatids. BMC Cell Biol. 10: 34.


Majava V. & Kursula P. (2009) Domain swapping and different oligomeric states for the complex between calmodulin and the calmodulin-binding domain of calcineurin A. PLoS ONE 4: e5402.


Bertini I., Kursula P., Luchinat C., Parigi G., Vahokoski J., Wilmanns M. & Yuan J. (2009) Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examples. J. Am. Chem. Soc. 131: 5134-5144.


Haikarainen T., Chen W.-Q., Lubec G. & Kursula P. (2009) Structure, modifications, and ligand-binding properties of rat profilin 2a. Acta Cryst. D 65: 303-311.


Zhang Z., Majava V., Greffier A., Hayes R.L., Kursula P. & Wang K.K.W. (2009) Collapsin response mediator protein-2 is a calmodulin binding protein.Cell. Mol. Life Sci. 66: 526-536.


2008

Meriläinen G., Schmitz W., Wierenga R. & Kursula P. (2008) The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme. FEBS J. 275: 6136-6148.


Kursula I., Kursula P., Ganter M., Panjikar S., Matuschewski K. & Schüler H. (2008) Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum. Structure 16: 1638-1648.


Majava V., Löytynoja N., Chen W.-Q., Lubec G. & Kursula P. (2008) Crystal and solution structure, stability, and post-translational modifications of collapsin response mediator protein 2. FEBS J. 275: 4583-4596.


Majava V., Petoukhov M.V., Hayashi N., Pirilä P., Svergun D.I. & Kursula P. (2008) Interaction between the C-terminal region of human myelin basic protein and calmodulin: Analysis of complex formation and solution structure. BMC Struct. Biol. 8: 10.


Kursula P. (2008) Structural properties of proteins specific to the myelin sheath. Amino Acids 34: 175-185.


Kursula P., Kursula I., Massimi M., Song Y.-H., Downer J., Stanley W.A., Witke W. & Wilmanns M. (2008) High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: the formin homology 1 domain of mDia1 and the proline-rich domain of VASP. J. Mol. Biol. 375: 270-290.


2007

Kursula P. & Majava V. (2007) A structural insight into lead neurotoxicity and calmodulin activation by heavy metals. Acta Cryst. F 63: 653-656.


Fukao T., Kursula P., Owen E.P. & Kondo N. (2007) Identification and characterization of a temperature-sensitive R268H mutation in the human succinyl-CoA:3-ketoacid CoA transferase (SCOT) gene. Mol. Genet. Metab. 92: 216-221.


Stanley W.A., Pursiainen N.V., Garman E.F., Juffer A.H., Wilmanns M. & Kursula P. (2007) A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding. BMC Struct. Biol. 7: 24.


Stenmark P., Ogg D., Flodin S., Flores A., Kotenyova T., Nyman T., Nordlund P. & Kursula P. (2007) The structure of human collapsin response mediator protein 2, a regulator of axonal growth. J. Neurochem. 101: 906-917.


Stenmark P., Kursula P., Flodin S., Gräslund S., Landry R., Nordlund P. & Schüler H. (2007) Crystal structure of human inosine triphosphatase: Substrate binding and implication of the ITPA deficiency mutation P32T. J. Biol. Chem. 282: 3182-3187.


2006

Stanley W.A., Filipp F.V., Kursula P., Schüller N., Erdmann R,. Schliebs W., Sattler M. & Wilmanns M. (2006) Recognition of a functional peroxisome type 1 target by the dynamic import receptor Pex5p. Mol. Cell 24: 653-663.


Kursula P., Flodin S., Ehn M., Hammarström M., Schüler H., Nordlund P. & Stenmark P. (2006) Crystal structure of the synthetase domain of human CTP synthetase, a target for anticancer therapy. Acta Cryst. F 62: 613-617.


Kursula P., Schüler H., Flodin S., Nilsson-Ehle P., Ogg D.J., Savitsky P., Nordlund P. & Stenmark P. (2006) Crystal structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue. Acta Cryst. D 62: 1294-1299.

2005

Kursula P., Sikkilä H., Fukao T., Kondo N. & Wierenga R.K. (2005) High resolution crystal structures of human cytosolic thiolase (CT). A comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I. J. Mol. Biol. 347: 189-201.

Kursula I., Heape, A.M. & Kursula P. (2005) Crystal structure of non-fused glutathione S-transferase from Schistosoma japonicum in complex with glutathione. Protein Pept. Lett. 12: 709-712.

Tzakos A.G., Kursula P., Theodorou V., Troganis A., Tselios T., Svarnas C., Matsoukas J., Apostopoulos V. & Gerothanassis I.P. (2005) Structure and function of the myelin proteins: Current status and perspectives in relation to multiple sclerosis. Curr. Med. Chem. 12: 1569-1587.

2004

Kursula P. (2004) XDSi - a graphical interface for the data processing program XDS. J. Appl. Cryst. 37: 347-348.

2003

Bhaumik P., Kursula P., Ratas V., Conzelmann E., Hiltunen J.K., Schmitz W. & Wierenga R.K. (2003) Crystallisation and preliminary X-ray diffraction analysis of 2-methylacyl-CoA racemase from Mycobacterium tuberculosis. Acta Cryst. D 59: 353-355.

Pekkala M., Hieta R., Kursula P., Kivirikko K.I., Wierenga R.K & Myllyharju J. (2003) Crystallization of the proline-rich-peptide binding domain of human type I collagen prolyl 4-hydroxylase. Acta Cryst. D 59: 940-942.

2002

Kursula P., Ojala J., Lambeir A.-M. & Wierenga R.K. (2002) The catalytic cycle of biosynthetic thiolase: A conformational journey of an acetyl group through four binding modes and two oxyanion holes. Biochemistry 41: 15543-15556.

2001

Kursula P., Lehto V.-P. & Heape A.M. (2001) The small myelin-associated glycoprotein binds to tubulin and microtubules. Mol. Brain Res. 87: 22-30.

Kursula P. (2001) The current status of structural studies on proteins of the myelin sheath. Int. J. Mol. Med. 8: 475-479.

2000

Kursula P., Lehto V.-P. & Heape A.M. (2000) Estimation of total ribonucleic acid quantity from dilute samples by nondenaturing electrophoresis and silver staining. Electrophoresis 21: 545-547.

Kursula P., Lehto V.-P. & Heape A.M. (2000) S100b inhibits the phosphorylation of the L-MAG cytoplasmic domain by PKA. Mol. Brain Res. 76: 407-410.

1999

Heape A. M., Lehto V.-P. & Kursula P. (1999) The expression of recombinant large myelin-associated glycoprotein cytoplasmic domain and the purification of native myelin-associated glycoprotein from rat brain and peripheral nerve. Prot. Express. Purif. 15:349-361.

Kursula P., Tikkanen G., Lehto V.-P., Nishikimi M. & Heape A.M. (1999) Calcium-dependent interaction between the large myelin-associated glycoprotein and S100b. J. Neurochem. 73: 1724-1732.

Kursula P., Meriläinen G., Lehto V.-P. & Heape A.M. (1999) The small myelin-associated glycoprotein is a zinc-binding protein. J. Neurochem. 73: 2110-2118.

1998

Kursula P., Lehto V.-P., Garbay B., Cassagne C. and Heape A.M. (1998) Expression of the amino acid dimorphism in the small myelin-associated glycoprotein cytoplasmic domain in rat peripheral nerves during postnatal development. Mol. Brain Res.54:252-261.

Publications in national current research information system (CRIStin)

We have set up a crystallization laboratory at the Deparment of Biomedicine recently. The current equipment includes: 

- crystallization robotics for soluble and membrane proteins (Mosquito LCP)

- temperature-controlled incubators at +8°C and +20°C

- several microscopes

- tools for crystal handling and transport to synchrotron sources

- a number of manual and electronic single- and multi-channel pipettes for manual crystallization

- a semi-automated 96-well liquid transfer tool 

- a good selection of different crystallization plates and screens

The facility is open for all users at UiB, and we will try to keep user costs at a minimum. We are happy to discuss collaborations, including all steps of the structure solution process.

Structural biology of the myelin sheath

Structural basis of neurological disease

High-resolution macromolecular crystallography 

Intrinsically disordered proteins

Protein-membrane interactions

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