The three‐dimensional structure of P2 myelin protein

• Published in: The EMBO journal Vol. 7; no. 6; pp. 1597 - 1604
• Main Authors: Jones, T. A., Bergfors, T., Sedzik, J., Unge, T.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 01-06-1988
• Subjects: Amino Acid Sequence; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Lipid Metabolism; Molecular biophysics; Molecular Sequence Data; myelin; Myelin Basic Protein - metabolism; Myelin P2 Protein; peripheral nervous system; Protein Conformation; Sequence Homology, Nucleic Acid; Structure in molecular biology; Tridimensional structure; X-Ray Diffraction; Proteins; Molecular structure; Myelin; Spatial structure; Conformation
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1988.tb02985.x

The three‐dimensional structure of P2 protein from peripheral nervous system myelin has been determined at 2.7 A resolution by X‐ray crystallography. The single isomorphous replacement/anomalous map was interpreted using skeletonized electron density on a computer graphics system. An atomic model was built using fragment fitting. The structure forms a compact 10‐stranded up‐and‐down beta‐barrel which encapsulates residual electron density that we interpret as a fatty acid molecule. This beta‐barrel shows some similarity to, but is different from, the retinol binding protein family of structures. The relationship of the P2 structure to a family of cytoplasmic, lipid binding proteins is described.