DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Ho Min | ko |
dc.contributor.author | Shin, DR | ko |
dc.contributor.author | Yoo, Ook-Joon | ko |
dc.contributor.author | Lee, H | ko |
dc.contributor.author | Lee, Jie-Oh | ko |
dc.date.accessioned | 2013-03-06T04:32:48Z | - |
dc.date.available | 2013-03-06T04:32:48Z | - |
dc.date.created | 2012-06-18 | - |
dc.date.created | 2012-06-18 | - |
dc.date.issued | 2003-03 | - |
dc.identifier.citation | FEBS LETTERS, v.538, no.1-3, pp.65 - 70 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | http://hdl.handle.net/10203/85805 | - |
dc.description.abstract | 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. | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | PEPTIDYL-DIPEPTIDASE | - |
dc.subject | MOLECULAR-CLONING | - |
dc.subject | MELANOGASTER | - |
dc.subject | HOMOLOG | - |
dc.subject | EXPRESSION | - |
dc.subject | ACER | - |
dc.subject | CARBOXYPEPTIDASE | - |
dc.subject | IDENTIFICATION | - |
dc.subject | INHIBITORS | - |
dc.subject | HYDROLYSIS | - |
dc.title | Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril | - |
dc.type | Article | - |
dc.identifier.wosid | 000181567200012 | - |
dc.identifier.scopusid | 2-s2.0-0037434846 | - |
dc.type.rims | ART | - |
dc.citation.volume | 538 | - |
dc.citation.issue | 1-3 | - |
dc.citation.beginningpage | 65 | - |
dc.citation.endingpage | 70 | - |
dc.citation.publicationname | FEBS LETTERS | - |
dc.identifier.doi | 10.1016/S0014-5793(03)00128-5 | - |
dc.contributor.localauthor | Kim, Ho Min | - |
dc.contributor.localauthor | Yoo, Ook-Joon | - |
dc.contributor.localauthor | Lee, Jie-Oh | - |
dc.contributor.nonIdAuthor | Shin, DR | - |
dc.contributor.nonIdAuthor | Lee, H | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | angiotensin I-converting enzyme | - |
dc.subject.keywordAuthor | angiotensin | - |
dc.subject.keywordAuthor | captopril | - |
dc.subject.keywordAuthor | lisinopril | - |
dc.subject.keywordAuthor | X-ray crystal structure | - |
dc.subject.keywordPlus | PEPTIDYL-DIPEPTIDASE | - |
dc.subject.keywordPlus | MOLECULAR-CLONING | - |
dc.subject.keywordPlus | MELANOGASTER | - |
dc.subject.keywordPlus | HOMOLOG | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | ACER | - |
dc.subject.keywordPlus | CARBOXYPEPTIDASE | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | INHIBITORS | - |
dc.subject.keywordPlus | HYDROLYSIS | - |
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