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PDBsum entry 1mw4
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protein ligands links
Hormone/growth factor/transferase PDB id
1mw4

 

 

 

 

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Contents
Protein chain
120 a.a. *
Ligands
PRO-GLN-PRO-GLU-
PTR-VAL-ASN-GLN-
PRO-ASP
* Residue conservation analysis
PDB id:
1mw4
Name: Hormone/growth factor/transferase
Title: Solution structure of the human grb7-sh2 domain in complex with a 10 amino acid peptide py1139
Structure: Growth factor receptor-bound protein 7. Chain: a. Fragment: sh2 domain. Synonym: grb7 adapter protein, epidermal growth factor receptor grb- 7, b47. Engineered: yes. Receptor protein-tyrosine kinase erbb-2. Chain: b. Fragment: sh2 domain binding site.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide was chemically synthesized. The sequence of the peptide is naturally found in homo sapiens (human).
NMR struc: 10 models
Authors: M.Ivancic,B.A.Lyons
Key ref: M.Ivancic et al. (2003). Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2. J Biomol Nmr, 27, 205-219. PubMed id: 12975581
Date:
27-Sep-02     Release date:   09-Sep-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q14451  (GRB7_HUMAN) -  Growth factor receptor-bound protein 7 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		532 a.a.
120 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.1  - receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-tyrosyl-[protein]
 + ATP
 = O-phospho-L-tyrosyl-[protein]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
J Biomol Nmr 27:205-219 (2003)
PubMed id: 12975581  
 
 
Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2.
M.Ivancic, R.J.Daly, B.A.Lyons.
 
  ABSTRACT  
 
The solution structure of the hGrb7-SH2 domain in complex with a ten amino acid phosphorylated peptide ligand representative of the erbB2 receptor tyrosine kinase (pY1139) is presented as determined by nuclear magnetic resonance methods. The hGrb7-SH2 domain structure reveals the Src homology 2 domain topology consisting of a central beta-sheet capped at each end by an alpha-helix. The presence of a four residue insertion in the region between beta-strand E and the EF loop and resulting influences on the SH2 domain/peptide complex structure are discussed. The binding conformation of the erbB2 peptide is in a beta-turn similar to that found in phosphorylated tyrosine peptides bound to the Grb2-SH2 domain. To our knowledge this is only the second example of an SH2 domain binding its naturally occurring ligands in a turn, instead of extended, conformation. Close contacts between residues responsible for binding specificity in hGrb7-SH2 and the erbB2 peptide are characterized and the potential effect of mutation of these residues on the hGrb7-SH2 domain structure is discussed.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18853468 S.Siamakpour-Reihani, H.J.Argiros, L.J.Wilmeth, L.L.Haas, T.A.Peterson, D.L.Johnson, C.B.Shuster, and B.A.Lyons (2009).
The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner.
  J Mol Recognit, 22, 9.  
18058821 J.S.McMurray (2008).
Structural basis for the binding of high affinity phosphopeptides to Stat3.
  Biopolymers, 90, 69-79.  
17705331 A.M.Spuches, H.J.Argiros, K.H.Lee, L.L.Haas, S.C.Pero, D.N.Krag, P.P.Roller, D.E.Wilcox, and B.A.Lyons (2007).
Calorimetric investigation of phosphorylated and non-phosphorylated peptide ligand binding to the human Grb7-SH2 domain.
  J Mol Recognit, 20, 245-252.  
17894853 C.J.Porter, J.M.Matthews, J.P.Mackay, S.E.Pursglove, J.W.Schmidberger, P.J.Leedman, S.C.Pero, D.N.Krag, M.C.Wilce, and J.A.Wilce (2007).
Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation.
  BMC Struct Biol, 7, 58.
PDB code: 2qms
15841400 C.J.Porter, M.C.Wilce, J.P.Mackay, P.Leedman, and J.A.Wilce (2005).
Grb7-SH2 domain dimerisation is affected by a single point mutation.
  Eur Biophys J, 34, 454-460.  
16243711 L.J.Holt, and R.J.Daly (2005).
Adapter protein connections: the MRL and Grb7 protein families.
  Growth Factors, 23, 193-201.  
15930003 M.Ivancic, A.M.Spuches, E.C.Guth, M.A.Daugherty, D.E.Wilcox, and B.A.Lyons (2005).
Backbone nuclear relaxation characteristics and calorimetric investigation of the human Grb7-SH2/erbB2 peptide complex.
  Protein Sci, 14, 1556-1569.  
15465854 K.Moncoq, I.Broutin, C.T.Craescu, P.Vachette, A.Ducruix, and D.Durand (2004).
SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer?
  Biophys J, 87, 4056-4064.  
15322292 P.J.Scharf, J.Witney, R.Daly, and B.A.Lyons (2004).
Solution structure of the human Grb14-SH2 domain and comparison with the structures of the human Grb7-SH2/erbB2 peptide complex and human Grb10-SH2 domain.
  Protein Sci, 13, 2541-2546.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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