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Abstract：
The tripeptide Arg-Gly-Asp acid (RGD) is a protein sequence in the binding of proteins to cell surfaces, and is involved in various biological processes such as cell adhesion to the extracellular matrix, platelet activation, hemostasis, etc. The C2 domain of the Von Willebrand Factor (VWF), containing the RGD motif, plays an important role in the initial homeostasis process. It binds to the αIIbβ3 integrin and stimulates platelet aggregation. We have investigated, using the molecular Dynamic (MD) simulation method, the effect of the RGD-peptide length, and temperature variation, on the binding to the αIIbβ3 integrin receptor. We examined 10 different structural modes of the αIIbβ3 at three different temperatures; 237 K, 310 K and 318 K. Our findings show that the amino acids that form a binding pocket include Asp224, Tyr234, Ser226, Tyr190, Tyr189, Trp260, Trp262, Asp259, Lys253, Arg214, Asp217, Ser161 and Ala218 and that the ligand-receptor interaction was increased at higher temperatures. It was also found that the increase in the number of ligands\' amino acids and their types (% glycine) plays an important role in the stability, conformation, and ligand-receptor interaction.Communicated by Ramaswamy H. Sarma.
摘要：
三肽Arg-Gly-Asp酸（RGD）是蛋白质与细胞表面结合的蛋白质序列，并参与各种生物过程，如细胞粘附到细胞外基质，血小板活化,止血,等。血管性血友病因子(VWF)的C2域，包含RGD图案，在初始稳态过程中起着重要作用。它与αIIbβ3整联蛋白结合并刺激血小板聚集。我们已经调查过了,采用分子动力学(MD)模拟方法,RGD-肽长度的影响，和温度变化，与αIIbβ3整合素受体的结合。我们在三个不同的温度下检查了αIIbβ3的10种不同的结构模式；237K，310K和318K。我们的发现表明，形成结合袋的氨基酸包括Asp224，Tyr234，Ser226，Tyr190，Tyr189，Trp260，Trp262，Asp259，Lys253，Arg214，Asp217，Ser161和Ala218，并且配体-受体相互作用在较高温度下增加。还发现配体氨基酸及其类型（％甘氨酸）的数量增加在稳定性中起重要作用，构象,和配体-受体相互作用。由RamaswamyH.Sarma沟通。
