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FEBS Lett. 2006 Mar 20;580(7):1872-6. Epub 2006 Feb 28.

Methionine acts as a "magnet" in photoaffinity crosslinking experiments.

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  • 1Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave, M&V 7, Boston, MA 02111, USA. Angela.Wittelsberger@tufts.edu


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 11 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.

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