ACTIN-BINDING PROTEIN COMPLEXES AT ATOMIC-RESOLUTION

被引：14

作者：

MCLAUGHLIN, PJ ^{[1
]}

WEEDS, AG ^{[1
]}

机构：

[1] MRC,MOLEC BIOL LAB,CAMBRIDGE CB2 2QH,ENGLAND

来源：

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1995年 / 24卷

基金：

英国惠康基金;

关键词：

G-ACTIN-BINDING PROTEINS; DNASE I; PROFILIN; GELSOLIN; PROTEIN CRYSTALLOGRAPHY;

D O I：

10.1146/annurev.bb.24.060195.003235

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This review describes three structures of actin complexed with different monomer-binding proteins, namely with DNase I, gelsolin segment 1, and profilin. In these proteins, the binding sites are discontinuous in the sequence, and those residues that form intermolecular hydrogen bonds are not well conserved in homologous proteins. The strongly conserved residues that define the family of proteins in gelsolin and profilin reflect the underlying structural fold of each. The binding surfaces for segment I and profilin are different, although they peripherally overlap on actin. No extreme features in the binding surfaces of these complexes distinguish them from other globular proteins.

引用

页码：643 / 675

页数：33

共 94 条

[1] LEFT-HANDED POLYPROLINE-II HELICES COMMONLY OCCUR IN GLOBULAR-PROTEINS [J].