Towards a complete atomic structure of spectrin family proteins

被引:48
作者
Broderick, MJF [1 ]
Winder, SJ [1 ]
机构
[1] Univ Glasgow, Inst Biomed & Life Sci, Glasgow Cell Biol Grp, Glasgow G12 8QQ, Lanark, Scotland
关键词
alpha-actinin; actin binding; alpha-spectrin; beta-spectrin; CH domain; coiled-coil; dystrophin; EF-hands; PH domain; SH3; domain; structure; utrophin; WW domain; ZZ domain;
D O I
10.1006/jsbi.2002.4465
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
The spectrin family of proteins represents a discrete group of cytoskeletal proteins comprising principally a-actinin, spectrin, dystrophin, and homologues and isoforms. They all share three main structural and functional motifs, namely, the spectrin repeat, EF-hands, and a CH domain-containing actin-binding domain. These proteins are variously involved in organisation of the actin cytoskeleton, membrane cytoskeleton architecture, cell adhesion, and contractile apparatus. The highly modular nature of these molecules has been a hindrance to the determination of their complete structures due to the inherent flexibility imparted on the proteins, but has also been an asset, inasmuch as the individual modules were of a size amenable to structural analysis by both crystallographic and NMR approaches. Representative structures of all the major domains shared by spectrum family proteins have now been solved at atomic resolution, including in some cases multiple domains from several family members. High-resolution structures, coupled with lower resolution methods to determine the overall molecular shape of these proteins, allow us for the first time to build complete atomic structures of the spectrum family of proteins. (C) 2002 Elsevier Science (USA).
引用
收藏
页码:184 / 193
页数:10
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