CH DOMAINS REVISITED

Citation
T. Stradal et al., CH DOMAINS REVISITED, FEBS letters, 431(2), 1998, pp. 134-137
Citations number
20
Categorie Soggetti
Biology,"Cell Biology",Biophysics
Journal title
ISSN journal
00145793
Volume
431
Issue
2
Year of publication
1998
Pages
134 - 137
Database
ISI
SICI code
0014-5793(1998)431:2<134:>2.0.ZU;2-D
Abstract
A sequence motif of about 100 amino acids, termed the 'calponin homolo gy 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 identif ied to date. We propose that single calponin homology domains do not c onfer actin-binding per se and that the actin-binding motifs of crossl inking proteins, which comprise two disparate calponin homology domain s, represent a unique protein module, (C) 1998 Federation of European Biochemical Societies.