Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin

被引:32
作者
Bramham, J
Hodgkinson, JL
Smith, BO
Uhrin, D
Barlow, PN
Winder, SJ
机构
[1] Univ Leicester, Dept Biochem, Leicester LE1 7RH, Leics, England
[2] Natl Heart & Lung Inst, Imperial Coll Sch Sci Technol & Med, London SW3 6LY, England
[3] Univ Edinburgh, Inst Cell & Mol Biol, Edinburgh EH9 3JR, Midlothian, Scotland
[4] Univ Edinburgh, Dept Chem, Edinburgh EH9 3JJ, Midlothian, Scotland
[5] Univ Glasgow, Inst Biomed & Life Sci, Div Biochem & Mol Biol, Glasgow G12 8QQ, Lanark, Scotland
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
actin binding; calponin-homology domain; NMR; structure; calponin;
D O I
10.1016/S0969-2126(02)00703-7
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
Calponin is involved in the regulation of contractility and organization of the actin cytoskeleton in smooth muscle cells. It is the archetypal member of the calponin homology (CH) domain family of actin binding proteins that includes cytoskeletal linkers such as alpha-actinin, spectrin and dystrophin, and regulatory proteins including VAV: IQGAP, and calponin. We have determined the first structure of a CH domain from a single CH domain-containing protein, that of calponin, and have fitted the NMR-derived coordinates to the 3D-helical reconstruction of the F-actin:calponin complex using cryoelectron microscopy. The tertiary fold of this single CH domain is typical of, yet significantly different from, those of the CH domains that occur in tandem pairs to form high-affinity ABDs in other proteins. We thus provide a structural insight into the mode of interaction between F-actin and CH domain-containing proteins.
引用
收藏
页码:249 / 258
页数:10
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