The three-dimensional structure of P2 myelin protein.
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.
Jones
T A
TA
Department of Molecular Biology, Biomedical Centre, Uppsala, Sweden.
Bergfors
T
T
Sedzik
J
J
Unge
T
T
D000595:Amino Acid Sequence; D050356:Lipid Metabolism; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000378:metabolism; D018996:Myelin P2 Protein; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
D004676:Myelin Basic Protein; D018996:Myelin P2 Protein