Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 26, Pages 9049-9057Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja101868c
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Funding
- Centre National de la Recherche Scientifique (CNRS)
- Paris-7 University
- E.U. [LSHG-CT-2005-513770]
- French Ministry of Research [ANR-06-BLAN-0087, ANR BLAN07-1/_191475]
- CNRS
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G protein-coupled receptors (GPCRs) are key players in signal recognition and cell communication and are among the most important targets for drug development. Direct structural information on the conformation of GPCR ligands bound to their receptors is scarce Using a leukotriene receptor, BLT2, expressed under a perdeuterated form in Escherichia colt, purified in milligram amounts, and folded to its native state using amphipols, we have solved, by H-1 NMR, the structure of receptor-bound leukotriene B4 (LTB4) Upon binding, LTB4 adopts a highly constrained seahorse conformation, at variance with the free state, where it explores a wide range of conformations. This structure provides an experimentally determined template of a pro-inflammatory compound for further pharmacological studies The novel approach used for its determination could prove powerful to investigate ligand binding to GPCRs and membrane proteins in general.
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