PDZ结构域的结构特点及其识别特异性配体的机制  

Structural Characterization of PDZ Domains and Molecular Mechanism of Their Recognition by Specific Ligands

作　　者：李华[1] 林葵[1] 吴更[1] 

机构地区：[1]上海交通大学生命科学技术学院,微生物代谢国家重点实验室,上海200240

出　　处：《中国生物化学与分子生物学报》2011年第12期1107-1112,共6页Chinese Journal of Biochemistry and Molecular Biology

基　　金：国家自然科学基金项目(No.30900225,30821005,90919021);上海市教育委员会科技创新项目(No.09ZZ23);上海市曙光计划(No.08SG11)~~

摘　　要：PDZ结构域作为介导蛋白质之间相互作用的重要结构域之一,参与到细胞内运输、离子通道、以及各种信号传导通路等多种生物学过程.PDZ结构域是由80～100个氨基酸组成的小的球状结构域,对某些多PDZ结构域蛋白来说,需要一前一后形成串联体才能正确折叠.另外,PDZ结构域相互之间也可以形成同源或异源二聚体.这些PDZ结构域的突出特点是能特异性地识别配体靶蛋白C末端短的氨基酸序列,但有些也能识别靶蛋白的内部β发夹结构.而一些支架蛋白的PDZ结构域与细胞膜上脂类的相互作用则增加了其与膜的亲和性.本文简要概括了PDZ结构域的结构特点及其对配体的各种特异性识别的机制,从而为研究各种PDZ蛋白的功能提供了结构基础.PDZ domains are one class of important protein-protein recognition modules that regulate multiple biological processes such as intracellular transport,ion channels,and various signal transduction pathways.PDZ domains are small globular domains composed of 80~100 amino acid residues.Some PDZ domains repeated in multi-PDZ proteins need to connect in a tandem arrangement to fold properly.Other PDZ domains can also bind to each other to form homo-or hetero-dimers.These domains specifically recognize short peptide motifs at the extreme C-terminal of target proteins,but some domains can bind to internal sequences folded in a β-hairpin structure.The interactions of PDZ domains in some scaffold proteins with membrane lipids increase their affinity to membrane.This review discussed the structural characterization of PDZ domains and the molecular mechanism of their recognition by specific ligands.These results provide a structural basis for understanding the function of PDZ-containing proteins.

关 键 词：PDZ结构域 PDZ-PDZ二聚体 配体 内部序列 

分 类 号：Q51[生物学—生物化学]