Zhou Q, Dangelmaier C, Smith J B
Department of Pharmacology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
Biochem Biophys Res Commun. 1996 Feb 27;219(3):720-6. doi: 10.1006/bbrc.1996.0301.
Catrocollastatin, a 50 kDa snake venom protein purified from Crotalus atrox, specifically inhibits platelet-collagen adhesion and collagen-induced aggregation. Catrocollastatin is composed of an N-terminal domain, a metalloproteinase domain, a disintegrin-like domain and a cysteine-rich C-terminal domain. The present studies show that catrocollastatin exerts its effect by binding to collagen. Based on the amino acid sequence and homology analysis, a cyclic oligopeptide corresponding to a conservative fragment containing the sequence SECD in the disintegrin-like domain has been synthesized. Like its protein parent, the synthetic peptide inhibits collagen-induced aggregation and possesses the ability to bind to collagen. This is the first snake venom protein with a disintegrin-like structure shown to bind to an integrin ligand matrix molecule instead of an integrin.
卡特罗抑素是一种从西部菱斑响尾蛇毒液中纯化得到的50 kDa蛇毒蛋白，它能特异性抑制血小板与胶原蛋白的黏附以及胶原蛋白诱导的聚集。卡特罗抑素由一个N端结构域、一个金属蛋白酶结构域、一个类去整合素结构域和一个富含半胱氨酸的C端结构域组成。目前的研究表明，卡特罗抑素通过与胶原蛋白结合发挥作用。基于氨基酸序列和同源性分析，合成了一种与类去整合素结构域中包含SECD序列的保守片段相对应的环寡肽。与它的蛋白母体一样，合成肽能抑制胶原蛋白诱导的聚集，并具有与胶原蛋白结合的能力。这是首个被证明能与整合素配体基质分子而非整合素结合的具有类去整合素结构的蛇毒蛋白。
