PDBsum entry 1dnq

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protein links
Transferase PDB id
Protein chain
312 a.a.
Theoretical model
PDB id:
Name: Transferase
Title: Theoretical model of the first and second domains of the human epidermal growth factor receptor ectodomain
Structure: Epidermal growth factor receptor. Chain: a. Fragment: l1 and s1 domains. Ec:
Source: Homo sapiens. Human
Authors: R.N.Jorissen,V.C.Epa,H.R.Treutlein,T.P.J.Garrett,C.W.Ward, A.W.Burgess
Key ref: R.N.Jorissen et al. (2000). Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor. Protein Sci, 9, 310-324. PubMed id: 10716183 DOI: 10.1110/ps.9.2.310
16-Dec-99     Release date:   12-Apr-00    
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Protein chain
Pfam   ArchSchema ?
P00533  (EGFR_HUMAN) -  Epidermal growth factor receptor
1210 a.a.
312 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.  - Transferred entry: and
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate

+ a
Molecule diagrams generated from .mol files obtained from the KEGG ftp site


DOI no: 10.1110/ps.9.2.310 Protein Sci 9:310-324 (2000)
PubMed id: 10716183  
Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor.
R.N.Jorissen, V.C.Epa, H.R.Treutlein, T.P.Garrett, C.W.Ward, A.W.Burgess.
The Epidermal Growth Factor (EGF) receptor is a tyrosine kinase that mediates the biological effects of ligands such as EGF and transforming growth factor alpha. An understanding of the molecular basis of its action has been hindered by a lack of structural and mutational data on the receptor. We have constructed comparative models of the four extracellular domains of the EGF receptor that are based on the structure of the first three domains of the insulin-like growth factor-1 (IGF-1) receptor. The first and third domains of the EGF receptor, L1 and L2, are right-handed beta helices. The second and fourth domains of the EGF receptor, S1 and S2, consist of the modules held together by disulfide bonds, which, except for the first module of the S1 domain, form rod-like structures. The arrangement of the L1 and S1 domains of the model are similar to that of the first two domains of the IGF-1 receptor, whereas that of the L2 and S2 domains appear to be significantly different. Using the EGF receptor model and limited information from the literature, we have proposed a number of regions that may be involved in the functioning of the receptor. In particular, the faces containing the large beta sheets in the L1 and L2 domains have been suggested to be involved with ligand binding of EGF to its receptor.

Literature references that cite this PDB file's key reference

  PubMed id Reference
12569553 Y.L.Yip, J.Novotny, M.Edwards, and R.L.Ward (2003).
Structural analysis of the ErbB-2 receptor using monoclonal antibodies: Implications for receptor signalling.
  Int J Cancer, 104, 303-309.  
11985614 J.H.Kim, K.Saito, and S.Yokoyama (2002).
Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin.
  Eur J Biochem, 269, 2323-2329.  
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