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IF

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Structure paper

TitleA comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 434, Page 191-196, Year 2013
Publish dateDec 4, 2012 (structure data deposition date)
AuthorsNabeno, M. / Akahoshi, F. / Kishida, H. / Miyaguchi, I. / Tanaka, Y. / Ishii, S. / Kadowaki, T.
External linksBiochem. Biophys. Res. Commun. / PubMed:23501107
MethodsX-ray diffraction
Resolution2.36 Å
Structure data

PDB-3w2t:
Crystal structure of human depiptidyl peptidase IV (DPP-4) in complex with vildagliptin
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

Chemicals

ChemComp-LF7:
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 / inhibitor*YM

ChemComp-GOL:
GLYCEROL

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / ALPHA/BETA / BETA-PROPELLER / HYDROLASE / AMINOPEPTIDASE / SERINE PROTEASE / SECRETED / SIGNAL-ANCHOR / TRANSMEMBRANE / DIABETES / GLYCOPROTEIN / CELL MEMBRANE / HYDROLASE-HYDROLASE INHIBITOR complex

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