CRYSTAL STRUCTURE OF ANCE-K26 COMPLEX
[ACE_DROME] May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.
Publication Abstract from PubMed
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 1.96A 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.
Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster.,Akif M, Ntai I, Sturrock ED, Isaac RE, Bachmann BO, Acharya KR Biochem Biophys Res Commun. 2010 Jul 30;398(3):532-6. Epub 2010 Jul 1. PMID:20599761
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.