Research

Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster


Reference:

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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Official URL:

http://dx.doi.org/10.1016/j.bbrc.2010.06.113

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.

Details

Item Type Articles
CreatorsAkif, M., Ntai, I., Sturrock, E. D., Isaac, R. E., Bachmann, B. O. and Acharya, K. R.
DOI10.1016/j.bbrc.2010.06.113
Uncontrolled Keywordsinhibitor binding, drosophila melanogaster, angiotensin converting enzyme, x-ray crystallography, zinc metallopeptidase
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedNo
StatusPublished
ID Code20564

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