Stradal T, Kranewitter W, Winder S J, Gimona M
Institute of Molecular Biology, Austrian Academy of Sciences, Department of Cell Biology, Salzburg.
FEBS Lett. 1998 Jul 17;431(2):134-7. doi: 10.1016/s0014-5793(98)00751-0.
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.
一种约100个氨基酸的序列基序,称为“钙调蛋白同源结构域”,已被认为能使肌动蛋白与多种细胞骨架和信号分子结合。在此,我们分析并比较了迄今鉴定出的所有含钙调蛋白同源结构域的蛋白质的序列。我们提出,单个钙调蛋白同源结构域本身并不赋予肌动蛋白结合能力,而交联蛋白的肌动蛋白结合基序由两个不同的钙调蛋白同源结构域组成,代表了一种独特的蛋白质模块。