Structural highlights
Function
MYP2_HORSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Equine P2 protein has been isolated from horse spinal cord and its structure determined to 2.1 A. 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 (Rfree=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.
Structure of myelin P2 protein from equine spinal cord.,Hunter DJ, Macmaster R, Roszak AW, Riboldi-Tunnicliffe A, Griffiths IR, Freer AA Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1067-71. Epub 2005, Jul 20. PMID:16041071[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hunter DJ, Macmaster R, Roszak AW, Riboldi-Tunnicliffe A, Griffiths IR, Freer AA. Structure of myelin P2 protein from equine spinal cord. Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1067-71. Epub 2005, Jul 20. PMID:16041071 doi:http://dx.doi.org/10.1107/S0907444905014162