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TitleDesign, synthesis and structure-activity relationships of novel biarylamine-based Met kinase inhibitors.
Journal, issue, pagesBioorg. Med. Chem. Lett., Vol. 20, Page 2998-3002, Year 2010
Publish dateJan 4, 2010 (structure data deposition date)
AuthorsWilliams, D.K. / Chen, X.T. / Tarby, C. / Kaltenbach, R. / Cai, Z.W. / Tokarski, J.S. / An, Y. / Sack, J.S. / Wautlet, B. / Gullo-Brown, J. ...Williams, D.K. / Chen, X.T. / Tarby, C. / Kaltenbach, R. / Cai, Z.W. / Tokarski, J.S. / An, Y. / Sack, J.S. / Wautlet, B. / Gullo-Brown, J. / Henley, B.J. / Jeyaseelan, R. / Kellar, K. / Manne, V. / Trainor, G.L. / Lombardo, L.J. / Fargnoli, J. / Borzilleri, R.M.
External linksBioorg. Med. Chem. Lett. / PubMed:20382527
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-3l8v:
Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor C-MET in complex with a biarylamine based inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-L8V:
2-({4-[(2-aminopyridin-4-yl)oxy]-3-fluorophenyl}amino)-N-(2,4-difluorophenyl)pyridine-3-carboxamide

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / RECEPTOR TYROSINE KINASE / SIGNAL TRANSDUCTION / GRB2 / SHC / ATP-BINDING / GLYCOPROTEIN / MEMBRANE / NUCLEOTIDE-BINDING / PHOSPHOPROTEIN / PROTO-ONCOGENE / TRANSMEMBRANE / TYROSINE-PROTEIN KINASE / Alternative splicing / Chromosomal rearrangement / Disease mutation / Kinase / Polymorphism / Receptor

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