Unique binding mode of Evogliptin with human dipeptidyl peptidase IV
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Hyung Ki | - |
dc.contributor.author | Kim, Mi-Kyung | - |
dc.contributor.author | Kim, Ha Dong | - |
dc.contributor.author | Kim, Heung Jae | - |
dc.contributor.author | Kim, Ji Won | - |
dc.contributor.author | Lee, Jie-Oh | - |
dc.contributor.author | Kim, Chan-Wha | - |
dc.contributor.author | Kim, Eunice EunKyeong | - |
dc.date.accessioned | 2021-09-02T21:52:40Z | - |
dc.date.available | 2021-09-02T21:52:40Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-12-16 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/81160 | - |
dc.description.abstract | Evogliptin ((R)-4-((R)-3-amino-4-(2,4,5-trifluorophenyl)butanoyl)-3-(tert-butoxymethyl)piperazine-2-one)) is a highly potent selective inhibitor of dipeptidyl peptidase IV (DPP4) that was approved for the treatment of type 2 diabetes in South Korea. In this study, we report the crystal structures of Evogliptin, DA-12166, and DA-12228 (S,R diastereomer of Evogliptin) complexed to human DPP4. Analysis of both the structures and inhibitory activities suggests that the binding of the trifluorophenyl moiety in the S-1 pocket and the piperazine-2-one moiety have hydrophobic interactions with Phe357 in the S-2 extensive subsite, and that the multiple hydrogen bonds made by the (R)-beta-amine group in the S-2 pocket and the contacts made by the (R)-tert-butyl group with Arg125 contribute to the high potency observed for Evogliptin. (c) 2017 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | HIGHLY POTENT | - |
dc.subject | PRECLINICAL PROFILE | - |
dc.subject | INHIBITOR | - |
dc.subject | DISCOVERY | - |
dc.subject | SYSTEM | - |
dc.title | Unique binding mode of Evogliptin with human dipeptidyl peptidase IV | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Chan-Wha | - |
dc.identifier.doi | 10.1016/j.bbrc.2017.10.101 | - |
dc.identifier.scopusid | 2-s2.0-85032980700 | - |
dc.identifier.wosid | 000416393300005 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.494, no.3-4, pp.452 - 459 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 494 | - |
dc.citation.number | 3-4 | - |
dc.citation.startPage | 452 | - |
dc.citation.endPage | 459 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | HIGHLY POTENT | - |
dc.subject.keywordPlus | PRECLINICAL PROFILE | - |
dc.subject.keywordPlus | INHIBITOR | - |
dc.subject.keywordPlus | DISCOVERY | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordAuthor | Dipeptidyl peptidase IV | - |
dc.subject.keywordAuthor | DPP4 | - |
dc.subject.keywordAuthor | Evogliptin | - |
dc.subject.keywordAuthor | Diabetes | - |
dc.subject.keywordAuthor | Inhibitor | - |
dc.subject.keywordAuthor | Complex structure | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.