SH3 domains: complexity in moderation.

SH3 domains: complexity in moderation.
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发表时间:
2001-04
影响因子:
4
通讯作者:
B. Mayer
B. Mayer
中科院分区:
生物学2区
文献类型:
--
作者:
B. Mayer

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SH3结构域可能是不断增长的蛋白质相互作用模块家族中最具特征的成员。这些结构域以中等亲和力和选择性结合富含脯氨酸的配体,在多种生物过程中发挥关键作用,包括通过分子内相互作用调节酶,增加局部浓度或改变信号通路组分的亚细胞定位,以及介导大型多蛋白复合物的组装。SH3结构域及其结合位点在从酵母到人类的数百种蛋白质中突然出现,这表明它们为细胞提供了一种特别方便和适应性强的将蛋白质聚集在一起的方式。丰富的遗传、生化和结构信息提供了该结构域的亲密和详细的描述,作为理解其他模块化蛋白质相互作用结构域的框架。由SH3结构域调控的过程也提出了关于特异性的本质和控制蛋白质相互作用网络的整体逻辑的重要问题。
The SH3 domain is perhaps the best-characterized member of the growing family of protein-interaction modules. By binding with moderate affinity and selectivity to proline-rich ligands, these domains play critical roles in a wide variety of biological processes ranging from regulation of enzymes by intramolecular interactions, increasing the local concentration or altering the subcellular localization of components of signaling pathways, and mediating the assembly of large multiprotein complexes. SH3 domains and their binding sites have cropped up in many hundreds of proteins in species from yeast to man, which suggests that they provide the cell with an especially handy and adaptable means of bringing proteins together. The wealth of genetic, biochemical and structural information available provides an intimate and detailed portrait of the domain, serving as a framework for understanding other modular protein-interaction domains. Processes regulated by SH3 domains also raise important questions about the nature of specificity and the overall logic governing networks of protein interactions.