DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Ho Min | - |
dc.contributor.author | Shin, DongRyel | - |
dc.contributor.author | Yoo, OokJoon | - |
dc.contributor.author | Lee, Hayyoung | - |
dc.contributor.author | Lee, Jie-Oh | - |
dc.date.accessioned | 2009-09-24T06:21:54Z | - |
dc.date.available | 2009-09-24T06:21:54Z | - |
dc.date.issued | 2003-03-13 | - |
dc.identifier.citation | FEBS LETTERS, Vol.538, No.1-3, pp.65-70 | en |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | http://hdl.handle.net/10203/11493 | - |
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. | en |
dc.description.sponsorship | The authors thank the sta¡ at the Cornell High Energy Synchrotron Source for assistance in data collection. This study was supported by a grant of the Korea Health 21 RpD Project, Ministry of Healthand Welfare, Republic of Korea (01-PJ1-PG3- 20900-0029). | en |
dc.language.iso | en_US | en |
dc.publisher | Elsevier | en |
dc.subject | PEPTIDYL-DIPEPTIDASE | en |
dc.subject | MOLECULAR-CLONING | en |
dc.subject | MELANOGASTER | en |
dc.subject | HOMOLOG | en |
dc.subject | EXPRESSION | en |
dc.subject | ACER | en |
dc.subject | CARBOXYPEPTIDASE | en |
dc.subject | IDENTIFICATION | en |
dc.subject | INHIBITORS | en |
dc.subject | HYDROLYSIS | en |
dc.title | Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril | en |
dc.type | Article | en |
dc.identifier.doi | 10.1016/S0014-5793(03)00128-5 | - |
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