PDZ domains and the formation of protein networks at the plasma membrane.
PDZ domains and the formation of protein networks at the plasma membrane.
复制标题
DOI：
10.1007/978-3-642-80481-6_9
复制
发表时间：
1998
影响因子：
--
通讯作者：
A. Fanning;J. Anderson
中科院分区：
文献类型：
--
作者：
A. Fanning;J. Anderson
蛋白质-蛋白质缔合是细胞结构和功能的大分子组织的基础。存在两种实现结合特异性的一般机制：“表面-表面”和”模块结构域-肽”缔合。前者是基于每对结合伴侣独特的相互作用表面化学，例如血红蛋白单体的寡聚化。表面-表面相互作用提供了高度特异性的结合，但这些协会的复杂性质并没有提供进化的机会，产生结合的多样性。相比之下，”模块化结构域-肽”关联基于保守结构域，其识别简单肽基序的变化。模块化结构域和肽靶都被发现是具有不同功能的多结构域蛋白质（例如酶、受体、细胞骨架蛋白）中的基序。这些结构域的实例包括充分表征的SH 3、SH 2和PTB结构域。
Protein-protein associations are the basis of much of the macromolecular organization underlying cellular structure and function. Two general mechanisms exist to achieve binding specificity:" surface-surface" and" modular domain-peptide" associations. The former is based on interacting surface chemistry unique to each pair of binding partners, eg, oligomerization of hemoglobin monomers. Surface-surface interactions provide for highly specific binding, but the complex nature of these associations has not provided evolution with the opportunity to generate binding diversity. In contrast," modular domain-peptide" associations are based on conserved domains which recognize variations of simple peptide motifs. Both the modular domains and peptide targets are found as motifs within multi domain proteins of diverse function, eg, enzymes, receptors, cytoskeletal proteins. Examples of these domains include the well characterized SH3, SH2 and PTB domains.