THE 3-DIMENSIONAL STRUCTURE OF P2 MYELIN PROTEIN
THE 3-DIMENSIONAL STRUCTURE OF P2 MYELIN PROTEIN
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DOI：
10.1002/j.1460-2075.1988.tb02985.x
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发表时间：
1988-06-01
期刊：
影响因子：
11.4
通讯作者：
UNGE, T
中科院分区：
文献类型：
--
作者：
JONES, TA;BERGFORS, T;UNGE, T
周围神经系统髓鞘质 P2 蛋白的三维结构已确定为 2.7 ANG。通过 X 射线晶体学分辨率。使用计算机图形系统上的骨架电子密度来解释单个同晶替换/异常图。使用片段拟合建立原子模型。该结构形成紧凑的10链上下β-桶，其封装了我们将其解释为脂肪酸分子的残余电子密度。该β-桶与视黄醇结合蛋白家族的结构显示出一些相似性，但又有所不同。描述了 P2 结构与细胞质脂质结合蛋白家族的关系。
The three-dimensional structure of P2 protein from peripheral nervous system myelin has been determined at 2.7 .ANG. resolution by X-ray crystallography. The single isomorphous replacement/anomalous map was interpreted using skeletonized electron density on a computer graphics system. An atomic model was built using fragment fitting. The structure forms a compact 10-stranded up-and-down .beta.-barrel which encapsulates residual electron density that we interpret as a fatty acid molecule. This .beta.-barrel shows some similarity to, but is different from, the retinol binding protein family of structures. The relationship of the P2 structure to a family of cytoplasmic, lipid binding proteins is described.