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Discovery of non-covalent dipeptidyl peptidase IV inhibitors which induce a conformational change in the active site

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Sheehan, Scott M. Mest, Hans-Juergen Watson, Brian M. Klimkowski, Valentine J. Timm, David E. Weichert, Andreas G.

A series of non-covalent inhibitors of the serine protease dipeptidyl peptidase IV (DPP-IV) were found to adopt a U-shaped binding conformation in X-ray co-crystallization studies. Remarkably, Tyr547 undergoes a 70 degrees side-chain rotation to accommodate the inhibitor and allows access to a previously unexposed area of the protein backbone for hydrogen bonding. (c) 2007 Elsevier Ltd. All rights reserved.

Document type Article de périodique (Journal article) – Article de recherche
Access type Accès restreint
Publication date 2007
Language Anglais
Journal information "Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology" - Vol. 17, no. 6, p. 1765-1768 (2007)
Peer reviewed yes
Publisher Pergamon-elsevier Science Ltd (Oxford)
issn 0960-894X
e-issn 1464-3405
Affiliation UCL
Keywords dipeptidyl peptidase IV ; protease inhibitor ; X-ray co-crystal structure ; oral glucose tolerance test
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Bibliographic reference Sheehan, Scott M. ; Mest, Hans-Juergen ; Watson, Brian M. ; Klimkowski, Valentine J. ; Timm, David E. ; et. al. Discovery of non-covalent dipeptidyl peptidase IV inhibitors which induce a conformational change in the active site. In: Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology, Vol. 17, no. 6, p. 1765-1768 (2007)
Permanent URL http://hdl.handle.net/2078.1/37668