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Structure paper

TitleThe selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 138, Page 514-524, Year 2009
Publish dateMar 24, 2009 (structure data deposition date)
AuthorsBae, J.H. / Lew, E.D. / Yuzawa, S. / Tome, F. / Lax, I. / Schlessinger, J.
External linksCell(Cambridge,Mass. ) / PubMed:19665973
MethodsX-ray diffraction
Resolution2.5 - 2.8 Å
Structure data

PDB-3gqi:
Crystal Structure of activated receptor tyrosine kinase in complex with substrates
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3gql:
Crystal Structure of activated receptor tyrosine kinase in complex with substrates
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-DVT:
DECAVANADATE

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GQL:
(E)-[4-(3,5-difluorophenyl)-3H-pyrrolo[2,3-b]pyridin-3-ylidene](3-methoxyphenyl)methanol

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
KeywordsTransferase/Transferase inhibitor / phosphorylated kinase / pY-recognition / tandem SH2 domains / ATP analog / ATP-binding / Craniosynostosis / Disease mutation / Disulfide bond / Dwarfism / Glycoprotein / Heparin-binding / Hypogonadotropic hypogonadism / Immunoglobulin domain / Kallmann syndrome / Kinase / Membrane / Nucleotide-binding / Phosphoprotein / Receptor / Transferase / Transmembrane / Tyrosine-protein kinase / Hydrolase / Lipid degradation / SH2 domain / SH3 domain / Transducer / Transferase-Transferase Inhibitor COMPLEX / activation

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