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PDBsum entry 3rhk
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Transferase/transferase inhibitor
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PDB id
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3rhk
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PDB id:
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Transferase/transferase inhibitor
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Title:
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Crystal structure of the catalytic domain of c-met kinase in complex with arq 197
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Structure:
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Hepatocyte growth factor receptor. Chain: a, b. Fragment: unp residues 1038-1346. Synonym: hgf receptor, hgf/sf receptor, proto-oncogenE C-met, scatter factor receptor, sf receptor, tyrosine-protein kinase met. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: met. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.94Å
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R-factor:
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0.203
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R-free:
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0.254
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Authors:
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S.Eathiraj,R.Palma,E.Volckova,M.Hirschi,D.S.France,M.A.Ashwell, T.C.Chan
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Key ref:
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S.Eathiraj
et al.
(2011).
Discovery of a novel mode of protein kinase inhibition characterized by the mechanism of inhibition of human mesenchymal-epithelial transition factor (c-Met) protein autophosphorylation by ARQ 197.
J Biol Chem,
286,
20666-20676.
PubMed id:
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Date:
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11-Apr-11
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Release date:
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27-Apr-11
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PROCHECK
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Headers
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References
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P08581
(MET_HUMAN) -
Hepatocyte growth factor receptor from Homo sapiens
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Seq:
Struc:
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1390 a.a.
298 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.7.10.1
- receptor protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Biol Chem
286:20666-20676
(2011)
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PubMed id:
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Discovery of a novel mode of protein kinase inhibition characterized by the mechanism of inhibition of human mesenchymal-epithelial transition factor (c-Met) protein autophosphorylation by ARQ 197.
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S.Eathiraj,
R.Palma,
E.Volckova,
M.Hirschi,
D.S.France,
M.A.Ashwell,
T.C.Chan.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Peters,
and
A.A.Adjei
(2012).
MET: a promising anticancer therapeutic target.
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Nat Rev Clin Oncol,
9,
314-326.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
