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3GQI

Crystal Structure of activated receptor tyrosine kinase in complex with substrates

Summary for 3GQI
Entry DOI10.2210/pdb3gqi/pdb
Related3GQL
DescriptorBasic fibroblast growth factor receptor 1, Phospholipase C-gamma-1, DECAVANADATE, ... (6 entities in total)
Functional Keywordsphosphorylated 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, transferase/transferase inhibitor
Biological sourceHomo sapiens (human)
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Cellular locationCell membrane; Single-pass type I membrane protein: P11362
Cell projection, lamellipodium : P10686
Total number of polymer chains2
Total formula weight65292.33
Authors
Bae, J.H.,Lew, E.D.,Yuzawa, S.,Tome, F.,Lax, I.,Schlessinger, J. (deposition date: 2009-03-24, release date: 2009-08-18, Last modification date: 2023-11-22)
Primary citationBae, J.H.,Lew, E.D.,Yuzawa, S.,Tome, F.,Lax, I.,Schlessinger, J.
The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site.
Cell(Cambridge,Mass.), 138:514-524, 2009
Cited by
PubMed: 19665973
DOI: 10.1016/j.cell.2009.05.028
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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