期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 398, 期 3, 页码 532-536出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.06.113
关键词
Angiotensin converting enzyme; Zinc metallopeptidase; X-ray crystallography; Inhibitor binding; Drosophila melanogaster
资金
- Medical Research Council (UK) [81272]
- Royal Society (UK)
- Medical Research Council [G0601973] Funding Source: researchfish
- MRC [G0601973] Funding Source: UKRI
Angiotensin-I converting enzyme (ACE, a zinc dependent dipeptidyl carboxypeptidase) is a major target of drugs due to its role in the modulation of blood pressure and cardiovascular disorders. Here we present a crystal structure of AnCE (an ACE homologue from Drosophila melanogaster with a single enzymatic domain) in complex with a natural product-phosphonotripeptide. K-26 at 1.96 angstrom resolution. The inhibitor binds exclusively in the S-1 and S-2 binding pockets of AnCE (coordinating the zinc ion) through ionic and hydrogen bond interactions. A detailed structural comparison of AnCE-K-26 complex with individual domains of human somatic ACE provides useful information for further exploration of ACE inhibitor pharmacophores involving phosphonic acids. (C) 2010 Elsevier Inc. All rights reserved.
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