6B1E

The structure of DPP4 in complex with Vildagliptin

Summary for 6B1E

• Entry DOI: 10.2210/pdb6b1e/pdb
• Descriptor: Dipeptidyl peptidase 4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-{[(1r,3s,5R,7S)-3-hydroxytricyclo[3.3.1.1~3,7~]decan-1-yl]amino}-1-{(2S)-2-[(E)-iminomethyl]pyrrolidin-1-yl}ethan-1-o ne, ... (6 entities in total)
• Functional Keywords: diabetes, dpp4 inhibitors, covalent inhibitors, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 173663.96

Authors

Scapin, G. (deposition date: 2017-09-18, release date: 2017-09-27, Last modification date: 2020-07-29)

Primary citation

Berger, J.P.,SinhaRoy, R.,Pocai, A.,Kelly, T.M.,Scapin, G.,Gao, Y.D.,Pryor, K.A.D.,Wu, J.K.,Eiermann, G.J.,Xu, S.S.,Zhang, X.,Tatosian, D.A.,Weber, A.E.,Thornberry, N.A.,Carr, R.D.
A comparative study of the binding properties, dipeptidyl peptidase-4 (DPP-4) inhibitory activity and glucose-lowering efficacy of the DPP-4 inhibitors alogliptin, linagliptin, saxagliptin, sitagliptin and vildagliptin in mice.
Endocrinol Diabetes Metab, 1:e00002-e00002, 2018

PubMed Abstract: Since 2006, DPP-4 inhibitors have become established therapy for the treatment of type 2 diabetes. Despite sharing a common mechanism of action, considerable chemical diversity exists amongst members of the DPP-4 inhibitor class, raising the question as to whether structural differences may result in differentiated enzyme inhibition and antihyperglycaemic activity.

PubMed: 30815539
DOI: 10.1002/edm2.2

Experimental method

X-RAY DIFFRACTION (1.77 Å)