CH domains revisited

FEBS Letters

Stradal, Theresia²  Gimona, Mario²  Kranewitter, Wolfgang²  Winder, Steven J¹ 

[1] Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK;Institute of Molecular Biology, Austrian Academy of Sciences, Department of Cell Biology, Billrothstrasse 11, A-5020 Salzburg, Austria

关键词: Calponin;    Calponin homology domain;    Actin binding;    CaP;    calponin;    CH domain;    calponin homology domain;    ABD;    actin binding domain;    CLR;    calponin-like repeat;   

DOI  :  10.1016/S0014-5793(98)00751-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A sequence motif of about 100 amino acids, termed the `calponin homology domain' has been suggested to confer actin binding to a variety of cytoskeletal and signalling molecules. Here we analyse and compare the sequences of all calponin homology domain-containing proteins identified to date. We propose that single calponin homology domains do not confer actin-binding per se and that the actin-binding motifs of cross-linking proteins, which comprise two disparate calponin homology domains, represent a unique protein module.

【 授权许可】

Unknown