Liddington Robert C
The Burnham Institute, La Jolla, CA, USA.
Methods Mol Biol. 2004;261:3-14. doi: 10.1385/1-59259-762-9:003.
Regulated interactions between proteins govern signaling pathways within and between cells. Although it is possible to derive some general principles of protein-protein recognition from experimentally determined structures, recent structural studies on protein complexes formed during signal transduction illustrate the remarkable diversity of interactions, both in terms of interfacial size and nature. There are two broad classes of complexes: "domain-domain," in which both components comprise prefolded structural units, and "domain-peptide," in which one component is a short motif that is unstructured in the absence of its binding partner. Signaling complexes often involve multidomain proteins whose multifaceted binding functions are regulated by intramolecular domain interactions. The structural basis of regulation, via steric and allosteric mechanisms, is discussed.
蛋白质之间的调控相互作用控制着细胞内和细胞间的信号通路。尽管可以从实验确定的结构中推导出一些蛋白质-蛋白质识别的一般原则，但最近对信号转导过程中形成的蛋白质复合物的结构研究表明，无论是在界面大小还是性质方面，相互作用都具有显著的多样性。复合物主要有两大类：“结构域-结构域”复合物，其中两个组分都包含预折叠的结构单元；“结构域-肽”复合物，其中一个组分是短基序，在没有结合伴侣时是无结构的。信号复合物通常涉及多结构域蛋白，其多方面的结合功能受分子内结构域相互作用的调控。本文讨论了通过空间位阻和变构机制进行调控的结构基础。
