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PDBsum entry 4hjo

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protein ligands links
Transferase/transferase inhibitor PDB id
4hjo
Jmol
Contents
Protein chain
278 a.a.
Ligands
AQ4
Waters ×34
PDB id:
4hjo
Name: Transferase/transferase inhibitor
Title: Crystal structure of the inactive egfr tyrosine kinase domai erlotinib
Structure: Epidermal growth factor receptor. Chain: a. Fragment: tyrosine kinase domain (unp residues 696-1022). Synonym: proto-oncogenE C-erbb-1, receptor tyrosine-protein erbb-1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: egfr, erbb, erbb1, her1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Resolution:
2.75Å     R-factor:   0.231     R-free:   0.253
Authors: J.H.Park,M.A.Lemmon
Key ref: J.H.Park et al. (2012). Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain. Biochem J, 448, 417-423. PubMed id: 23101586 DOI: 10.1042/BJ20121513
Date:
13-Oct-12     Release date:   14-Nov-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00533  (EGFR_HUMAN) -  Epidermal growth factor receptor
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1210 a.a.
278 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.2.7.10.1  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP
+ [protein]-L-tyrosine
= ADP
+ [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     protein phosphorylation   1 term 
  Biochemical function     transferase activity, transferring phosphorus-containing groups     4 terms  

 

 
    reference    
 
 
DOI no: 10.1042/BJ20121513 Biochem J 448:417-423 (2012)
PubMed id: 23101586  
 
 
Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain.
J.H.Park, Y.Liu, M.A.Lemmon, R.Radhakrishnan.
 
  ABSTRACT  
 
Erlotinib and gefitinib, tyrosine kinase inhibitors used to block EGFR (epidermal growth factor receptor) signalling in cancer, are thought to bind only the active conformation of the EGFR-TKD (tyrosine kinase domain). Through parallel computational and crystallographic studies, we show in the present study that erlotinib also binds the inactive EGFR-TKD conformation, which may have significant implications for its use in EGFR-mutated cancers.