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

M Akif, I Ntai, E D Sturrock, R E Isaac, B O Bachmann, K Ravi Acharya

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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.
Original languageEnglish
Pages (from-to)532-536
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 30 Jul 2010



  • inhibitor binding
  • drosophila melanogaster
  • angiotensin converting enzyme
  • x-ray crystallography
  • zinc metallopeptidase

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