2OQI
Human Dipeptidyl Peptidase IV (DPP4) with Piperidinone-constrained phenethylamine
Summary for 2OQI
| Entry DOI | 10.2210/pdb2oqi/pdb |
| Descriptor | Dipeptidyl peptidase 4 (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (TP103) (Adenosine deaminase complexing protein 2) (ADABP), (4R,5R)-5-AMINO-1-[2-(1,3-BENZODIOXOL-5-YL)ETHYL]-4-(2,4,5-TRIFLUOROPHENYL)PIPERIDIN-2-ONE (2 entities in total) |
| Functional Keywords | serine-peptidase, 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 | 4 |
| Total formula weight | 338242.84 |
| Authors | Pei, Z.,Li, X.,von Geldern, T.W.,Longenecker, K.L.,Pireh, D.,Stewart, K.D.,Backes, B.J.,Lai, C.,Lubben, T.H.,Ballaron, S.J.,Beno, D.W.,Kempf-Grote, A.J.,Sham, H.L.,Trevillyan, J.M. (deposition date: 2007-01-31, release date: 2007-04-03, Last modification date: 2024-11-13) |
| Primary citation | Pei, Z.,Li, X.,Geldern, T.W.,Longenecker, K.,Pireh, D.,Stewart, K.D.,Backes, B.J.,Lai, C.,Lubben, T.H.,Ballaron, S.J.,Beno, D.W.,Kempf-Grote, A.J.,Sham, H.L.,Trevillyan, J.M. Discovery and Structure-Activity Relationships of Piperidinone- and Piperidine-Constrained Phenethylamines as Novel, Potent, and Selective Dipeptidyl Peptidase IV Inhibitors. J.Med.Chem., 50:1983-1987, 2007 Cited by PubMed Abstract: Dipeptidyl peptidase IV (DPP4) inhibitors are emerging as a new class of therapeutic agents for the treatment of type 2 diabetes. They exert their beneficial effects by increasing the levels of active glucagon-like peptide-1 and glucose-dependent insulinotropic peptide, which are two important incretins for glucose homeostasis. Starting from a high-throughput screening hit, we were able to identify a series of piperidinone- and piperidine-constrained phenethylamines as novel DPP4 inhibitors. Optimized compounds are potent, selective, and have good pharmacokinetic profiles. PubMed: 17367123DOI: 10.1021/jm061436d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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