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Petri Kursula lab

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The function of biological molecules can only be fully understood when their structure and dynamics are known at the atomic level. We study various aspects of protein structure and protein-membrane interactions, and we use molecules from the vertebrate myelin sheath as our primary in vitro model system to understand the assembly of biomembranes at different levels of complexity. 

We focus on using different structural biology and biophysical methods to solve problems related to nervous system development and disease. While the main focus is on the molecules involved in the assembly of the myelin sheath, our scientific interests are broad. In addition to structural neurobiology, we enjoy membrane-binding proteins, intrinsically disordered molecules, X-rays and neutrons, and ultrahigh-resolution X-ray crystallography of macromolecules - to name but a few. 

New aspects of myelination
MAG-DYNLL1 complex

A novel protein interaction in myelin

One long-standing question in myelin biochemistry was solved, as a new binding partner specific for the large isoform of MAG was identified.

Synaptic protein structure
arc

Structure of the memory regulator Arc

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.

Molecules of myelination
CNPase

Unraveling the mysteries of myelin maturation

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.

High-resolution crystallography
Shank3-SH3

An SH3 domain like no other at the post-synaptic density

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...

Why UiB
A portrait of a male student standing outside a building

Study biomedical sciences in modern Norway

What is it like to study and work within the biomedical sciences in Norway?

We are part of the Neurotargeting Research Group at the Department of Biomedicine.