Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 35, Issue 9, Pages 471-475Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2010.03.006
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Funding
- National Institutes of Health [GM064700]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM064700] Funding Source: NIH RePORTER
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Structures of the influenza A virus M2 proton channel in the open conformation have been determined by X-ray crystallography, and in the closed conformation by NMR. Whereas the X-ray structure shows a single inhibitor molecule in the middle of the channel, four inhibitor molecules bind the channel's outer surface in the NMR structure. In both structures, the strongest hot spots (i.e., regions that contribute substantially to the free energy of binding any potential ligand) lie inside the pore, and other hot spots are found at exterior locations. By considering all available models, we propose the primary drug binding site is inside the pore, but that exterior binding occurs under appropriate conditions.
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