PDBsum entry 3gql

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Transferase/transferase inhibitor PDB id
Protein chain
287 a.a. *
GQL ×3
Waters ×187
* Residue conservation analysis
PDB id:
Name: Transferase/transferase inhibitor
Title: Crystal structure of activated receptor tyrosine kinase in c with substrates
Structure: Basic fibroblast growth factor receptor 1. Chain: a, b, c. Fragment: protein kinase domain. Synonym: fgfr-1, bfgf-r, fms-like tyrosine kinase 2, c-fgr. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fgfbr, fgfr1, flg, flt2. Expressed in: escherichia coli. Expression_system_taxid: 562
2.80Å     R-factor:   0.252     R-free:   0.289
Authors: J.H.Bae,E.D.Lew,S.Yuzawa,F.Tome,I.Lax,J.Schlessinger
Key ref: J.H.Bae et al. (2009). The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell, 138, 514-524. PubMed id: 19665973
24-Mar-09     Release date:   18-Aug-09    
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Protein chains
Pfam   ArchSchema ?
P11362  (FGFR1_HUMAN) -  Fibroblast growth factor receptor 1
822 a.a.
287 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
+ [protein]-L-tyrosine
+ [protein]-L-tyrosine phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     signal transduction   5 terms 
  Biochemical function     transferase activity, transferring phosphorus-containing groups     6 terms  


Cell 138:514-524 (2009)
PubMed id: 19665973  
The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site.
J.H.Bae, E.D.Lew, S.Yuzawa, F.Tomé, I.Lax, J.Schlessinger.
SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. However, the modest binding affinity of SH2 domains to pY containing peptides may not account for and likely represents an oversimplified mechanism for regulation of selectivity of signaling pathways in living cells. Here we describe the crystal structure of the activated tyrosine kinase domain of FGFR1 in complex with a phospholipase Cgamma fragment. The structural and biochemical data and experiments with cultured cells show that the selectivity of phospholipase Cgamma binding and signaling via activated FGFR1 are determined by interactions between a secondary binding site on an SH2 domain and a region in FGFR1 kinase domain in a phosphorylation independent manner. These experiments reveal a mechanism for how SH2 domain selectivity is regulated in vivo to mediate a specific cellular process.