Structure of myelin P2 protein from equine spinal cord
Structure of myelin P2 protein from equine spinal cord
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DOI：
10.1107/s0907444905014162
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发表时间：
2005-08-01
影响因子：
2.2
通讯作者：
Freer, AA
中科院分区：
文献类型：
--
作者：
Hunter, DJB;Macmaster, R;Freer, AA
马P2蛋白已从马脊髓中分离出来，其结构确定为2.1埃。由于马髓磷脂是一种可行的替代牛组织的大规模制剂，表征的蛋白质从马脊髓髓磷脂已开始。与其他物种相比，马CNS髓鞘中P2蛋白的含量异常高。通过分子置换确定结构，随后将其精修至R值为0.187（无R = 0.233）。该结构在结合腔中含有去污剂LDAO和HEPES缓冲液的分子，并且在其他方面类似于其他细胞视黄醇结合蛋白。
Equine P2 protein has been isolated from horse spinal cord and its structure determined to 2.1 angstrom. 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.