Journal
FEBS LETTERS
Volume 580, Issue 7, Pages 1872-1876Publisher
WILEY
DOI: 10.1016/j.febslet.2006.02.050
Keywords
parathyroid hormone receptor-1; photoaffinity crosslinking; cyanogen bromide; methionine scan; site-directed mutagenesis
Funding
- NIDDK NIH HHS [DK-47940] Funding Source: Medline
- NIGMS NIH HHS [GM-54082] Funding Source: Medline
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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.
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