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Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster


Reference:

Akif, M., Masuyer, G., Bingham, R. J., Sturrock, E. D., Isaac, R. E. and Acharya, K. R., 2012. Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster. FEBS Journal, 279 (24), pp. 4525-4534.

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http://dx.doi.org/10.1111/febs.12038

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Abstract

Human somatic angiotensin-1 converting enzyme (ACE) is a zinc-dependent exopeptidase, that catalyses the conversion of the decapeptide angiotensin I to the octapeptide angiotensin II, by removing a C-terminal dipeptide. It is the principal component of the renin-angiotensin–aldosterone system that regulates blood pressure. Hence it is an important therapeutic target for the treatment of hypertension and cardiovascular disorders. Here, we report the structures of an ACE homologue from Drosophila melanogaster (AnCE; a proven structural model for the more complex human ACE) co-crystallized with mammalian peptide substrates (bradykinin, Thr6–bradykinin, angiotensin I and a snake venom peptide inhibitor, bradykinin-potentiating peptide-b). The structures determined at 2-Å resolution illustrate that both angiotensin II (the cleaved product of angiotensin I by AnCE) and bradykinin-potentiating peptide-b bind in an analogous fashion at the active site of AnCE, but also exhibit significant differences. In addition, the binding of Arg–Pro–Pro, the cleavage product of bradykinin and Thr6– bradykinin, provides additional detail of the general peptide binding in AnCE. Thus the new structures of AnCE complexes presented here improves our understanding of the binding of peptides and the mechanism by which peptides inhibit this family of enzymes.

Details

Item Type Articles
CreatorsAkif, M., Masuyer, G., Bingham, R. J., Sturrock, E. D., Isaac, R. E. and Acharya, K. R.
DOI10.1111/febs.12038
Related URLs
URLURL Type
http://www.scopus.com/inward/record.url?scp=84870489857&partnerID=8YFLogxKUNSPECIFIED
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code32966

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