2OGZ

Crystal structure of DPP-IV complexed with Lilly aryl ketone inhibitor

Summary for 2OGZ

• Entry DOI: 10.2210/pdb2ogz/pdb
• Descriptor: Dipeptidyl peptidase, 4-[(3R)-3-{[2-(4-FLUOROPHENYL)-2-OXOETHYL]AMINO}BUTYL]BENZAMIDE (3 entities in total)
• Functional Keywords: dipeptidyl peptidase iv, cd26, dpiv, dpp-iv, dpp4, serine protease, inhibitor, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Dipeptidyl peptidase 4 soluble form: Secreted . Cell membrane ; Single- pass type II membrane protein: P27487
• Total number of polymer chains: 2
• Total formula weight: 169582.00

Authors

Timm, D.E. (deposition date: 2007-01-09, release date: 2007-03-06, Last modification date: 2024-10-30)

Primary citation

Sheehan, S.M.,Mest, H.J.,Watson, B.M.,Klimkowski, V.J.,Timm, D.E.,Cauvin, A.,Parsons, S.H.,Shi, Q.,Canada, E.J.,Wiley, M.R.,Ruehter, G.,Evers, B.,Petersen, S.,Blaszczak, L.C.,Pulley, S.R.,Margolis, B.J.,Wishart, G.N.,Renson, B.,Hankotius, D.,Mohr, M.,Zechel, J.C.,Michael Kalbfleisch, J.,Dingess-Hammond, E.A.,Boelke, A.,Weichert, A.G.
Discovery of non-covalent dipeptidyl peptidase IV inhibitors which induce a conformational change in the active site.
Bioorg.Med.Chem.Lett., 17:1765-1768, 2007

PubMed Abstract: 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.

PubMed: 17239592
DOI: 10.1016/j.bmcl.2006.12.074

Experimental method

X-RAY DIFFRACTION (2.1 Å)