2RGU

Crystal structure of complex of human DPP4 and inhibitor

Summary for 2RGU

• Entry DOI: 10.2210/pdb2rgu/pdb
• Descriptor: Dipeptidyl peptidase 4, 2-acetamido-2-deoxy-beta-D-glucopyranose, 8-[(3R)-3-Aminopiperidin-1-yl]-7-but-2-yn-1-yl-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-d ione, ... (4 entities in total)
• Functional Keywords: peptidase, inhibitor, aminopeptidase, glycoprotein, hydrolase, membrane, protease, secreted, serine protease, signal-anchor, transmembrane
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 173297.76

Authors

Nar, H.,Himmelsbach, F.,Eckhardt, M. (deposition date: 2007-10-05, release date: 2007-11-06, Last modification date: 2024-10-30)

Primary citation

Eckhardt, M.,Langkopf, E.,Mark, M.,Tadayyon, M.,Thomas, L.,Nar, H.,Pfrengle, W.,Guth, B.,Lotz, R.,Sieger, P.,Fuchs, H.,Himmelsbach, F.
8-(3-(R)-Aminopiperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methyl-quinazolin-2-ylmethyl)-3,7-dihydropurine-2,6-dione (BI 1356), a Highly Potent, Selective, Long-Acting, and Orally Bioavailable DPP-4 Inhibitor for the Treatment of Type 2 Diabetes.
J.Med.Chem., 50:6450-6453, 2007

PubMed Abstract: A new chemical class of potent DPP-4 inhibitors structurally derived from the xanthine scaffold for the treatment of type 2 diabetes has been discovered and evaluated. Systematic structural variations have led to 1 (BI 1356), a highly potent, selective, long-acting, and orally active DPP-4 inhibitor that shows considerable blood glucose lowering in different animal species. 1 is currently undergoing clinical phase IIb trials and holds the potential for once-daily treatment of type 2 diabetics.

PubMed: 18052023
DOI: 10.1021/jm701280z

Experimental method

X-RAY DIFFRACTION (2.6 Å)