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https://olympias.lib.uoi.gr/jspui/handle/123456789/9661Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Tzakos, A. G. | en |
| dc.contributor.author | Naqvi, N. | en |
| dc.contributor.author | Comporozos, K. | en |
| dc.contributor.author | Pierattelli, R. | en |
| dc.contributor.author | Theodorou, V. | en |
| dc.contributor.author | Husain, A. | en |
| dc.contributor.author | Gerothanassis, I. P. | en |
| dc.date.accessioned | 2015-11-24T16:50:56Z | - |
| dc.date.available | 2015-11-24T16:50:56Z | - |
| dc.identifier.issn | 0960-894X | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9661 | - |
| dc.rights | Default Licence | - |
| dc.subject | angiotensin-converting enzyme | en |
| dc.subject | captopril | en |
| dc.subject | isomerization | en |
| dc.subject | mutagenesis | en |
| dc.subject | nmr | en |
| dc.subject | crystal-structure | en |
| dc.subject | domain | en |
| dc.subject | lisinopril | en |
| dc.subject | inhibitors | en |
| dc.subject | binding | en |
| dc.title | The molecular basis for the selection of captopril cis and trans conformations by angiotensin I converting enzyme | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | DOI 10.1016/j.bmcl.2006.07.034 | - |
| heal.identifier.secondary | <Go to ISI>://000240615400020 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0960894X06008092/1-s2.0-S0960894X06008092-main.pdf?_tid=a916c5e4-3a30-11e3-be14-00000aacb35f&acdnat=1382346822_2b15eb78a7a161b542c37de9619819c8 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2006 | - |
| heal.abstract | Enzyme-inhibitor recognition is considered one of the most fundamental aspects in the area of drug discovery. However, the molecular mechanism of this recognition process (induced fit or prebinding and adaptive selection among multiple conformers) in several cases remains unexplored. In order to shed light toward this step of the recognition process in the case of human angiotensin I converting enzyme (hACE) and its inhibitor captopril, we have established a novel combinatorial approach exploiting solution NMR, flexible docking calculations, mutagenesis, and enzymatic studies. We provide evidence that an equimolar ratio of the cis and trans states of captopril exists in solution and that the enzyme selects only the trans state of the inhibitor that presents architectural and stereoelectronic complementarity with its substrate binding groove. (c) 2006 Elsevier Ltd. All rights reserved. | en |
| heal.publisher | Elsevier | en |
| heal.journalName | Bioorganic and Medicinal Chemistry Letters | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Tzakos-2006-The molecular basis.pdf | 343.14 kB | Adobe PDF | View/Open Request a copy |
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