期刊论文详细信息
FEBS Letters | |
CH domains revisited | |
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
【 预 览 】
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RO201912020306221ZK.pdf | 588KB | download |