Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster
Akif, M., Ntai, I., Sturrock, E. D., Isaac, R. E., Bachmann, B. O. and Acharya, K. R., 2010. Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster. Biochemical and Biophysical Research Communications, 398 (3), pp. 532-536.
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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.
|Creators||Akif, M., Ntai, I., Sturrock, E. D., Isaac, R. E., Bachmann, B. O. and Acharya, K. R.|
|Uncontrolled Keywords||inhibitor binding,drosophila melanogaster,angiotensin converting enzyme,x-ray crystallography,zinc metallopeptidase|
|Departments||Faculty of Science > Biology & Biochemistry|
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