Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril

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Angiotensin I-converting enzymes (ACEs) are zinc metallopeptidases that cleave carboxy-terminal dipeptides from short peptide hormones. We have determined the crystal structures of AnCE, a Drosopkild homolog of ACE, with and without bound inhibitors to 2.4 Angstrom resolution. AnCE contains a large internal channel encompassing the entire protein molecule. This substrate-binding channel is composed of two chambers, reminiscent of a peanut shell. The inhibitor and zinc-binding sites are located in the narrow bottleneck connecting the two chambers. The substrate and inhibitor specificity of AnCE appears to be determined by extensive hydrogen-bonding networks and ionic interactions in the active site channel. The catalytically important zinc ion is coordinated by the conserved Glu395 and histidine residues from a HExxH motif. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Publisher
Elsevier
Issue Date
2003-03-13
Keywords

PEPTIDYL-DIPEPTIDASE; MOLECULAR-CLONING; MELANOGASTER; HOMOLOG; EXPRESSION; ACER; CARBOXYPEPTIDASE; IDENTIFICATION; INHIBITORS; HYDROLYSIS

Citation

FEBS LETTERS, Vol.538, No.1-3, pp.65-70

ISSN
0014-5793
DOI
10.1016/S0014-5793(03)00128-5
URI
http://hdl.handle.net/10203/11493
Appears in Collection
CH-Journal Papers(저널논문)

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