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Structure paper

Titlec-Met inhibitors with novel binding mode show activity against several hereditary papillary renal cell carcinoma-related mutations.
Journal, issue, pagesJ. Biol. Chem., Vol. 283, Page 2675-2683, Year 2008
Publish dateOct 1, 2007 (structure data deposition date)
AuthorsBellon, S.F. / Kaplan-Lefko, P. / Yang, Y. / Zhang, Y. / Moriguchi, J. / Rex, K. / Johnson, C.W. / Rose, P.E. / Long, A.M. / O'Connor, A.B. ...Bellon, S.F. / Kaplan-Lefko, P. / Yang, Y. / Zhang, Y. / Moriguchi, J. / Rex, K. / Johnson, C.W. / Rose, P.E. / Long, A.M. / O'Connor, A.B. / Gu, Y. / Coxon, A. / Kim, T.S. / Tasker, A. / Burgess, T.L. / Dussault, I.
External linksJ. Biol. Chem. / PubMed:18055465
MethodsX-ray diffraction
Resolution2.2 - 2.5 Å
Structure data

PDB-2rfn:
x-ray structure of c-Met with inhibitor.
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-2rfs:
X-ray structure of SU11274 bound to c-Met
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-AM7:
2-benzyl-5-(3-fluoro-4-{[6-methoxy-7-(3-morpholin-4-ylpropoxy)quinolin-4-yl]oxy}phenyl)-3-methylpyrimidin-4(3H)-one

ChemComp-HOH:
WATER

ChemComp-AM8:
N-(3-chlorophenyl)-N-methyl-2-oxo-3-[(3,4,5-trimethyl-1H-pyrrol-2-yl)methyl]-2H-indole-5-sulfonamide

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / c-Met HGF receptor tyrosine kinse kinase domain / ATP-binding / Glycoprotein / Membrane / Nucleotide-binding / Phosphorylation / Proto-oncogene / Transmembrane / Tyrosine-protein kinase / c-Met / receptor tyrosine kinase / SU11274

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