1RWQ

Human Dipeptidyl peptidase IV in complex with 5-aminomethyl-6-(2,4-dichloro-phenyl)-2-(3,5-dimethoxy-phenyl)-pyrimidin-4-ylamine

Summary for 1RWQ

• Entry DOI: 10.2210/pdb1rwq/pdb
• Related: 1NU6 1NU8
• Descriptor: Dipeptidyl peptidase IV, 2-acetamido-2-deoxy-beta-D-glucopyranose, 5-(AMINOMETHYL)-6-(2,4-DICHLOROPHENYL)-2-(3,5-DIMETHOXYPHENYL)PYRIMIDIN-4-AMINE, ... (4 entities in total)
• Functional Keywords: dipeptidyl peptidase iv, exopeptidase, adenosine binding, drug design, complex structure, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 171505.45

Authors

Hennig, M.,Thoma, R.,Stihle, M. (deposition date: 2003-12-17, release date: 2004-12-17, Last modification date: 2020-07-29)

Primary citation

Peters, J.U.,Weber, S.,Kritter, S.,Weiss, P.,Wallier, A.,Boehringer, M.,Hennig, M.,Kuhn, B.,Loeffler, B.M.
Aminomethylpyrimidines as novel DPP-IV inhibitors: a 10(5)-fold activity increase by optimization of aromatic substituents
Bioorg.Med.Chem.Lett., 14:1491-1493, 2004

PubMed Abstract: The influence of aromatic substitution on a newly discovered class of inhibitors of dipeptidyl peptidase IV was investigated. A 10(5)-fold increase in potency was achieved by the optimization of aromatic substituents in a parallel chemistry program. The observed SAR could be explained by an X-ray structure of the protein-ligand complex.

PubMed: 15006388
DOI: 10.1016/j.bmcl.2004.01.019

Experimental method

X-RAY DIFFRACTION (2.2 Å)