1yiv

Structure of myelin P2 protein from Equine spinal cord

spinqualitylabelsall models 1yiv, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1yiv is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: EPE, LDA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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