title: Structure of human ACE gives new insights into inhibitor binding and design.
abstract: Angiotensin-converting enzyme (ACE) is a primary target of drugs used for controlling hypertension. A new X-ray crystallographic structure of the key catalytic domain of ACE provides detailed information about the structure of its active site, located in a deep channel, and its interactions with an inhibitor. Such information might facilitate the rational design of ACE inhibitors that are more potent and more selective and therefore of clinical use.
authors.affiliation: Department of Biomedical Sciences, Florida Atlantic University, Boca Raton, FL 33431, USA. kbrew@fau.edu
authors.forename: Keith
authors.initials: K
authors.lastname: Brew
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D015195:Drug Design; D006801:Humans; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D007703:Peptidyl-Dipeptidase A