Structural highlights
Publication Abstract from PubMed
Several soil-derived actinobacteria produce secondary metabolites that are proven specific and potent inhibitors of the human angiotensin-I converting enzyme (ACE), a key target for the modulation of hypertension through its role in the renin-angiotensin-aldosterone system. K-26-DCP is a zinc dipeptidyl carboxypeptidase produced by Astrosporangium hypotensionis, and an ancestral homologue of ACE. Here we report the high resolution crystal structures of K-26-DCP and of its complex with the natural microbial tripeptide product K-26. The experimental results provide the structural basis for better understanding the specificity of K-26 for human ACE over bacterial DCPs. This article is protected by copyright. All rights reserved.
Crystal structure of a peptidyl-dipeptidase K-26-DCP from Actinomycete in complex with its natural inhibitor.,Masuyer G, Cozier GE, Kramer GJ, Bachmann BO, Acharya KR FEBS J. 2016 Oct 18. doi: 10.1111/febs.13928. PMID:27754586[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Masuyer G, Cozier GE, Kramer GJ, Bachmann BO, Acharya KR. Crystal structure of a peptidyl-dipeptidase K-26-DCP from Actinomycete in complex with its natural inhibitor. FEBS J. 2016 Oct 18. doi: 10.1111/febs.13928. PMID:27754586 doi:http://dx.doi.org/10.1111/febs.13928
