Open AccessStructure of myelin P2 protein from equine spinal cord
Author(s) -
Hunter Dominic J. B.,
Macmaster Rachel,
Roszak Aleksander W.,
RiboldiTunnicliffe Alan,
Griffiths Ian R.,
Freer Andrew A.
Publication year - 2005
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444905014162
Subject(s) - myelin , spinal cord , myelin basic protein , chemistry , central nervous system , anatomy , microbiology and biotechnology , biology , endocrinology , neuroscience
Equine P2 protein has been isolated from horse spinal cord and its structure determined to 2.1 Å. Since equine myelin is a viable alternative to bovine tissue for large‐scale preparations, characterization of the proteins from equine spinal cord myelin has been initiated. There is an unusually high amount of P2 protein in equine CNS myelin compared with other species. The structure was determined by molecular replacement and subsequently refined to an R value of 0.187 ( R free = 0.233). The structure contains a molecule of the detergent LDAO and HEPES buffer in the binding cavity and is otherwise analogous to other cellular retinol‐binding proteins.