1YIV

Structure of myelin P2 protein from Equine spinal cord

Summary for 1YIV

• Entry DOI: 10.2210/pdb1yiv/pdb
• Related: 1CBQ 1CRB 1PMP
• Descriptor: Myelin P2 protein, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, LAURYL DIMETHYLAMINE-N-OXIDE, ... (4 entities in total)
• Functional Keywords: p2 protein, lipid transport
• Biological source: Equus caballus (horse)
• Cellular location: Cytoplasm: P0C6G6
• Total number of polymer chains: 1
• Total formula weight: 14954.46

Authors

Hunter, D.J.B.,MacMaster, R.,Rozak, A.W.,Riboldi-Tunnicliffe, A.,Grifiths, I.R.,Freer, A.A. (deposition date: 2005-01-13, release date: 2005-07-26, Last modification date: 2023-10-25)

Primary citation

Hunter, D.J.,Macmaster, R.,Roszak, A.W.,Riboldi-Tunnicliffe, A.,Griffiths, I.R.,Freer, A.A.
Structure of myelin P2 protein from equine spinal cord.
Acta Crystallogr.,Sect.D, 61:1067-1071, 2005

PubMed Abstract: 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.

PubMed: 16041071
DOI: 10.1107/S0907444905014162

Experimental method

X-RAY DIFFRACTION (2.1 Å)