Structure of myelin P2 protein from equine spinal cord

Hunter DJB; Macmaster R; Roszak AWRiboldi-Tunnicliffe AGriffiths IRFreer AA

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Structure of myelin P2 protein from equine spinal cord

机译：从马脊髓髓P2蛋白结构绳

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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.

机译：从马马P2蛋白已被隔离2.1脊髓和其结构决定埃。牛组织大规模的替代品准备,蛋白质的表征从马脊髓髓磷脂启动。P2蛋白相比,马中枢神经系统髓鞘其他物种。随后分子置换和精制R值为0.187(有空= 0.233)。结构包含一个分子的洗涤剂绑定腔和LDAO和消息灵通的缓冲区另有类似于其他细胞吗retinol-binding蛋白质。

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来源
《Acta crystallographica.Section D. Biological crystallography》 |2005年第8期|1067-1071|共5页
作者
Hunter DJB; Macmaster R; Roszak AWRiboldi-Tunnicliffe AGriffiths IRFreer AA;
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作者单位

Univ Glasgow, Dept Chem, Glasgow G12 8QQ, Lanark, Scotland;

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原文格式 PDF
正文语种英语
中图分类化学;
关键词
integrating cavity; Tissue-specific expression; TretinoinmyelinPurificationSpinal CordEquidaeEquusRefiningMyelin P2 ProteinR-VALUERats;

机译：结合腔;组织表达式;TretinoinmyelinPurificationSpinal;

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Structure of myelin P2 protein from equine spinal cord

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