S100B与其蛋白靶点的钙依赖性相互作用。

Cardiovascular psychiatry and neurology Pub Date : 2010-01-01 Epub Date: 2010-08-17 DOI:10.1155/2010/728052
Danna B Zimmer, David J Weber
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引用次数: 58

摘要

S100B是一种钙信号蛋白,是S100蛋白家族的成员。S100B和大多数其他S100蛋白(S100s)的一个重要特征是,在没有蛋白靶标的情况下,它们通常与Ca(2+)离子结合相对较弱;在与目标蛋白结合后,Ca(2+)的结合就会增加200到400倍。本文综述了在蛋白靶点存在下Ca(2+)结合亲和力增加的结构基础和生理意义。关于家族成员之间的冗余以及介导S100B和其他S100s与其靶标相互作用的结构域的新信息也被提出。正是个体s100之间的多样性、它们与之相互作用的蛋白靶点以及这些蛋白-蛋白相互作用对Ca(2+)的依赖性,使得s100能够将[Ca(2+)](细胞内)水平的变化转化为空间和时间上独特的生物反应。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

The Calcium-Dependent Interaction of S100B with Its Protein Targets.

The Calcium-Dependent Interaction of S100B with Its Protein Targets.

The Calcium-Dependent Interaction of S100B with Its Protein Targets.

The Calcium-Dependent Interaction of S100B with Its Protein Targets.

S100B is a calcium signaling protein that is a member of the S100 protein family. An important feature of S100B and most other S100 proteins (S100s) is that they often bind Ca(2+) ions relatively weakly in the absence of a protein target; upon binding their target proteins, Ca(2+)-binding then increases by as much as from 200- to 400-fold. This manuscript reviews the structural basis and physiological significance of increased Ca(2+)-binding affinity in the presence of protein targets. New information regarding redundancy among family members and the structural domains that mediate the interaction of S100B, and other S100s, with their targets is also presented. It is the diversity among individual S100s, the protein targets that they interact with, and the Ca(2+) dependency of these protein-protein interactions that allow S100s to transduce changes in [Ca(2+)](intracellular) levels into spatially and temporally unique biological responses.

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