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-Structure paper
Title | c-Met inhibitors with novel binding mode show activity against several hereditary papillary renal cell carcinoma-related mutations. |
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Journal, issue, pages | J. Biol. Chem., Vol. 283, Page 2675-2683, Year 2008 |
Publish date | Oct 1, 2007 (structure data deposition date) |
Authors | 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. ...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 links | J. Biol. Chem. / PubMed:18055465 |
Methods | X-ray diffraction |
Resolution | 2.2 - 2.5 Å |
Structure data | PDB-2rfn: PDB-2rfs: |
Chemicals | ChemComp-AM7: ChemComp-HOH: ChemComp-AM8: |
Source |
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Keywords | TRANSFERASE / 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 |