Feinberg J, Lebart M, Benyamin Y, Roustan C
Centre de Recherches de Biochimie Macromoléculaire (CNRS), Laboratoirede Recherche sur la Motilité Cellulaire (Ecole Pratique des Hautes Etudes), Université de Montpellier 1, France.
Biochem Biophys Res Commun. 1997 Apr 7;233(1):61-5. doi: 10.1006/bbrc.1997.6402.
The binding of the N-terminal domain (S1) of gelsolin to monomeric actin has been extensively documented. In contrast, the location of the C-terminal calcium dependent domains (S4-6) interacting with the actin filament during the severing process remains uncertain. In this study, we have identified a new interface that supports calcium dependent gelsolin binding to actin. This site is located in a critical position towards actin-actin contact in the filament and in the vicinity of the phalloidin site. Using specific antibody and synthetic peptides derived from actin sequence within 105-132 residues, this interface was finally ascribed to the segment 112-120 on the actin subdomain-1.
凝溶胶蛋白的N端结构域(S1)与单体肌动蛋白的结合已有大量文献记载。相比之下,在切断过程中与肌动蛋白丝相互作用的C端钙依赖结构域(S4-6)的位置仍不确定。在本研究中,我们确定了一个新的界面,该界面支持钙依赖的凝溶胶蛋白与肌动蛋白结合。该位点位于肌动蛋白丝中肌动蛋白-肌动蛋白接触的关键位置,且靠近鬼笔环肽位点。利用特异性抗体和源自肌动蛋白序列105-132位残基的合成肽,该界面最终被确定为肌动蛋白亚结构域1上的112-120片段。