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Inhibitors of the catalytic domain of mitochondrial ATP synthase.

作者信息

Gledhill J R, Walker J E

机构信息

MRC Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, UK.

出版信息

Biochem Soc Trans. 2006 Nov;34(Pt 5):989-92. doi: 10.1042/BST0340989.


DOI:10.1042/BST0340989
PMID:17052243
Abstract

An understanding of the mechanism of ATP synthase requires an explanation of how inhibitors act. The catalytic F1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states. Four independent inhibitory sites have been identified by high-resolution structural studies. They are the catalytic site, and the binding sites for the antibiotics aurovertin and efrapeptin and for the natural inhibitor protein, IF1.

摘要

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