牛S100β蛋白的核磁共振归属及二级结构

Nuclear magnetic resonance assignments and secondary structure of bovine S100 beta protein.

作者信息

Kilby P M, Van Eldik L J, Roberts G C

机构信息

Department of Biochemistry, University of Leicester, UK.

出版信息

FEBS Lett. 1995 Apr 17;363(1-2):90-6. doi: 10.1016/0014-5793(95)00296-l.

DOI:10.1016/0014-5793(95)00296-l

PMID:7729560

Abstract

S100 beta is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100 beta. The secondary structure is similar to that of calbindin D9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue alpha-helix in S100 beta.

摘要

S100β是一种神经突延伸因子，与阿尔茨海默病和唐氏综合征有关。它属于一组含有螺旋-环-螺旋钙结合基序的低分子量钙结合蛋白。仅一种S100蛋白（钙结合蛋白D9k）的结构已被确定，它与S100组的其他成员具有最低的序列相似性。我们报告了无钙S100β的核磁共振（NMR）归属和二级结构。除了有明确证据表明S100β中存在一个额外的排列良好的5个残基的α螺旋外，其二级结构与通过核磁共振确定的钙结合蛋白D9k的二级结构相似。