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PDBsum entry 2ks1

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protein Protein-protein interface(s) links
Transferase PDB id
2ks1
Jmol
Contents
Protein chains
44 a.a. *
44 a.a. *
* Residue conservation analysis
PDB id:
2ks1
Name: Transferase
Title: Heterodimeric association of transmembrane domains of erbb1 receptors enabling kinase activation
Structure: Receptor tyrosine-protein kinase erbb-2. Chain: a. Fragment: erbb2tm domain, unp residues 641-684. Synonym: p185erbb2, c-erbb-2, neu proto-oncogene, tyrosine type cell surface receptor her2, mln 19. Engineered: yes. Epidermal growth factor receptor. Chain: b. Fragment: erbb1tm domain, unp residues 634-677.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: erbb2, her2, neu, ngl. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: egfr, erbb1. Expression_system_taxid: 562
NMR struc: 12 models
Authors: K.S.Mineev,E.V.Bocharov,Y.E.Pustovalova,O.V.Bocharova,V.V.Ch A.S.Arseniev
Key ref: K.S.Mineev et al. (2010). Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases. J Mol Biol, 400, 231-243. PubMed id: 20471394 DOI: 10.1016/j.jmb.2010.05.016
Date:
24-Dec-09     Release date:   09-Jun-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04626  (ERBB2_HUMAN) -  Receptor tyrosine-protein kinase erbB-2
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1255 a.a.
44 a.a.
Protein chain
Pfam   ArchSchema ?
P00533  (EGFR_HUMAN) -  Epidermal growth factor receptor
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1210 a.a.
44 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: 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

 

 
    reference    
 
 
DOI no: 10.1016/j.jmb.2010.05.016 J Mol Biol 400:231-243 (2010)
PubMed id: 20471394  
 
 
Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases.
K.S.Mineev, E.V.Bocharov, Y.E.Pustovalova, O.V.Bocharova, V.V.Chupin, A.S.Arseniev.
 
  ABSTRACT  
 
Growth factor receptor tyrosine kinases of the ErbB family play a significant role in vital cellular processes and various cancers. During signal transduction across plasma membrane, ErbB receptors are involved in lateral homodimerization and heterodimerization with proper assembly of their extracellular single-span transmembrane (TM) and cytoplasmic domains. The ErbB1/ErbB2 heterodimer appears to be the strongest and most potent inducer of cellular transformation and mitogenic signaling compared to other ErbB homodimers and heterodimers. Spatial structure of the heterodimeric complex formed by TM domains of ErbB1 and ErbB2 receptors embedded into lipid bicelles was obtained by solution NMR. The ErbB1 and ErbB2 TM domains associate in a right-handed alpha-helical bundle through their N-terminal double GG4-like motif T(648)G(649)X(2)G(652)A(653) and glycine zipper motif T(652)X(3)S(656)X(3)G(660), respectively. The described heterodimer conformation is believed to support the juxtamembrane and kinase domain configuration corresponding to the receptor active state. The capability for multiple polar interactions, along with hydrogen bonding between TM segments, correlates with the observed highest affinity of the ErbB1/ErbB2 heterodimer, implying an important contribution of the TM helix-helix interaction to signal transduction.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21474065 N.Jura, X.Zhang, N.F.Endres, M.A.Seeliger, T.Schindler, and J.Kuriyan (2011).
Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms.
  Mol Cell, 42, 9.  
21371926 Y.S.Choong, T.S.Lim, A.L.Chew, I.Aziah, and A.Ismail (2011).
Structural and functional studies of a 50 kDa antigenic protein from Salmonella enterica serovar Typhi.
  J Mol Graph Model, 29, 834-842.  
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