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A new high-resolution crystal structure of the Drosophila melanogaster angiotensin converting enzyme homologue, AnCE

DOI: 10.1016/j.fob.2015.08.004 DOI Help
PMID: 26380810 PMID Help

Authors: Charlotte Harrison (University of Bath) , K. Ravi Acharya (University of Bath)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Open Bio , VOL 5 , PAGES 661 - 667

State: Published (Approved)
Published: August 2015
Diamond Proposal Number(s): 8922

Open Access Open Access

Abstract: Angiotensin converting enzyme (ACE) is a zinc-dependent dipeptidyl carboxypeptidase with an essential role in blood pressure homeostasis in mammals. ACE has long been targeted in the treatment of hypertension through ACE inhibitors, however current inhibitors are known to cause severe side effects. Therefore, there is a requirement for a new generation of ACE inhibitors and structural information will be invaluable in their development. ACE is a challenging enzyme to work with due to its extensive glycosylation. As such, the Drosophila melanogaster ACE homologue, AnCE, which shares ∼60% sequence similarity with human ACE, can be used as a model for studying inhibitor binding. The presence of ligands originating from the crystallisation condition at the AnCE active site has proved an obstacle to studying the binding of new inhibitor precursors. Here we present the crystal structure of AnCE (in a new crystal form) at 1.85 Å resolution, using crystals grown under different conditions. This new structure may be more suitable for studying the binding of new compounds, with the potential of developing a new generation of improved ACE inhibitors.

Journal Keywords: X-Ray Crystallography; Crystal Structure; Angiotensin-I Converting Enzyme; Metalloprotease; Zinc Binding Protein; Inhibitor Binding

Subject Areas: Biology and Bio-materials

Instruments: I24-Microfocus Macromolecular Crystallography

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