Methionine acts as a "magnet" in photoaffinity crosslinking experiments
Methionine acts as a "magnet" in photoaffinity crosslinking experiments
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DOI：
10.1016/j.febslet.2006.02.050
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发表时间：
2006-03-20
期刊：
影响因子：
3.5
通讯作者：
Rosenblatt, M
中科院分区：
文献类型：
--
作者：
Wittelsberger, A;Thomas, BE;Rosenblatt, M
光亲和交联已被用来探测一些G蛋白偶联受体系统的配体-受体界面的性质。通常，发现掺入配体中的光反应性二苯甲酮部分与受体中的甲硫氨酸反应。我们将甲硫氨酸一次一个地引入甲状旁腺激素受体的163-176区域，并发现甲硫氨酸的侧链在一系列II氨基酸上发生交联。我们称之为蛋氨酸的“磁铁效应”。因此，受体结构域中甲硫氨酸的存在可显著改变交联接触点。(c)2006年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Photoaffinity crosslinking has been utilized to probe the nature of the ligand-receptor interface for a number of G protein-coupled receptor systems. Often the photoreactive benzophenone moiety incorporated in the ligand is found to react with a methionine in the receptor. We introduced methionines one-at-a-time into the region 163-176 of the parathyroid hormone receptor, and find that crosslinking occurs to the side-chain of methionine over a range of I I amino acids. We call this the '' Magnet Effect '' of methionine. Hence, crosslinking contact points can be significantly shifted by the presence of methionine in a receptor domain. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.