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Abstract
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.
Original language | English |
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Pages (from-to) | 532-536 |
Number of pages | 5 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 398 |
Issue number | 3 |
DOIs | |
Publication status | Published - 30 Jul 2010 |
Keywords
- inhibitor binding
- drosophila melanogaster
- angiotensin converting enzyme
- x-ray crystallography
- zinc metallopeptidase
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Dive into the research topics of 'Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster'. Together they form a unique fingerprint.Projects
- 1 Finished
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STRUCTURAL STUDIES ON HUMAN ANGIOTENSIN-I CONVERTING ENZYME
Acharya, R. (PI)
15/04/08 → 14/04/11
Project: Research council