Radel S J, Genco R J, De Nardin E
Department of Oral Biology, State University of New York, Buffalo.
Biochem Int. 1991 Nov;25(4):745-53.
The formyl peptide receptor is involved in the activation of human neutrophils (PMN) and their subsequent response to chemotactic peptides such as FMLP. The normal FMLP receptor has been reported to contain both high and low affinity states and to consist of several glycoprotein components, ranging in size from 40-94 kDa. However, little is known about the functional domains of the receptor. In this study we have constructed synthetic peptides corresponding to different portions of the reported receptor structure, and have tested their involvement in ligand binding. One of these peptides, corresponding to the first extracellular loop of the N-terminus end of the molecule, has been shown to specifically inhibit FMLP binding to PMN membranes. Concomitantly, this peptide exhibited the strongest direct binding to the ligand. We propose that this portion of the FMLP receptor molecule is important in receptor-ligand interactions.
甲酰肽受体参与人类中性粒细胞（PMN）的激活及其随后对趋化肽（如FMLP）的反应。据报道，正常的FMLP受体包含高亲和力和低亲和力状态，由几种糖蛋白成分组成，大小在40 - 94 kDa之间。然而，关于该受体的功能结构域知之甚少。在本研究中，我们构建了与报道的受体结构不同部分相对应的合成肽，并测试了它们在配体结合中的作用。其中一种肽对应于分子N末端的第一个细胞外环，已被证明能特异性抑制FMLP与PMN膜的结合。同时，该肽与配体表现出最强的直接结合。我们认为FMLP受体分子的这一部分在受体 - 配体相互作用中很重要。
