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PDBsum entry 1k37

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protein links
Hormone/growth factor PDB id
1k37
Jmol
Contents
Protein chain
46 a.a. *
* Residue conservation analysis
PDB id:
1k37
Name: Hormone/growth factor
Title: Nmr structure of human epiregulin
Structure: Epiregulin. Chain: a. Fragment: residues 1-46. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 1 models
Authors: K.Sato,K.Miura,M.Tada,T.Aizawa,K.Miyamoto,K.Kawano
Key ref:
K.Sato et al. (2003). Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity. FEBS Lett, 553, 232-238. PubMed id: 14572630 DOI: 10.1016/S0014-5793(03)01005-6
Date:
02-Oct-01     Release date:   30-Sep-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O14944  (EREG_HUMAN) -  Proepiregulin
Seq:
Struc:
169 a.a.
46 a.a.
Key:    PfamB domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/S0014-5793(03)01005-6 FEBS Lett 553:232-238 (2003)
PubMed id: 14572630  
 
 
Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity.
K.Sato, T.Nakamura, M.Mizuguchi, K.Miura, M.Tada, T.Aizawa, T.Gomi, K.Miyamoto, K.Kawano.
 
  ABSTRACT  
 
Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Tertiary structure of EPR. A: The ensemble of 40 NMR structures of EPR superimposed and fitted for the backbone atoms of residues 4–44. B: The ribbon drawing of the minimized average structure of EPR. Sequence numbers of some residues are indicated. These diagrams were generated using the program MOLMOL [30].
Figure 4.
Fig. 4. A: Comparison of the structure in the C-terminal domain between EPR and EGF. Hydrogen bonds between Ser^38 and Thr^44 in EGF are shown by continuous lines with the hydrogen bond lengths. The lengths between backbone NH and O atoms in EPR are shown by dotted lines. Backbone NH and O atoms are represented by blue and red, respectively. B: Comparison of the hydrogen bond lengths (Å) in the C-terminal domain among EGF-family ligands. The lengths between backbone NH and O atoms in EPR are shown for comparison.
 
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2003, 553, 232-238) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18199660 I.Iloro, D.Narváez, N.Guillén, C.M.Camacho, L.Guillén, E.Cora, and B.Pastrana-Ríos (2008).
The kinetics of the hydrogen/deuterium exchange of epidermal growth factor receptor ligands.
  Biophys J, 94, 4041-4055.  
17211472 C.M.McClelland, and W.J.Gullick (2007).
Proteomic identification of secreted proteins as surrogate markers for signal transduction inhibitor activity.
  Br J Cancer, 96, 284-289.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.