Home
Petri Kursula lab

News archive for Petri Kursula lab

Charcot-Marie-Tooth disease (CMT) is the most common inherited neuropathy in humans, linked to mutations in dozens of different genes. Two of these genes encode the proteins GDAP1 and NDRG1. We have solved the crystal structures of these two proteins, in order to better understand their structure, function, and involvement in disease.
Myelin, the insulative multilamellar sheath that enwraps axons, speeds up our nerve impulses by two orders of magnitude – a prerequisite for an efficient nervous system that we humans and other vertebrates enjoy. Myelin gains its structure and function from a high abundance of lipids and proteins, many of which are specific to this enigmatic biological system.
The ILL brochures are meant for the general public with a scientific interest, and they cover the application of neutron techniques in different areas of research. The "Neutrons in Health" brochure is published every 5 years, and 20 topics are selected globally from top research performed at the ILL (Grenoble, France). Two of these 20 highlights in the latest issue are from our work on... Read more
The candidate will give a trial lecture and defend his doctoral thesis with the title: “The Characterization of Disordered Membrane-Binding Proteins of Myelin: A Biophysical Approach"
One long-standing question in myelin biochemistry was solved, as a new binding partner specific for the large isoform of MAG was identified.
The post-synaptic protein Arc has been termed a master regulator of memory. In line with its homology to certain viral proteins, it has also been shown recently to form virus-like capsids. We have elucidated for the first time the 3D structure of full-length monomeric Arc.
The Shank family of proteins functions as a molecular scaffold in the neuronal post-synaptic density, enabling numerous protein-protein interactions. Shanks are large multi-domain molecules, and one of the conserved domains is an SH3 domain. Using high-resolution X-ray crystallography, we show that the SH3 domain in the Shank family has lost its canonical ligand-binding site.
The molecular processes of myelin maturation are to a large extent still unknown. A coordinated interplay between regulatory and functional molecules must take place for correct timing of myelin membrane apposition and compaction, such that cytoplasmic channels are also formed in a correct way.