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PDBsum entry 2j05

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protein Protein-protein interface(s) links
Signal transduction PDB id
2j05
Jmol
Contents
Protein chains
64 a.a. *
60 a.a. *
Waters ×117
* Residue conservation analysis
PDB id:
2j05
Name: Signal transduction
Title: Crystal structure of the rasgap sh3 domain at 1.5 angstrom resolution
Structure: Ras gtpase-activating protein 1. Chain: a, b. Fragment: sh3 domain, residues 281-341. Synonym: gtpase-activating protein, gap, ras p21 protein activator, p120gap, rasgap. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.50Å     R-factor:   0.177     R-free:   0.199
Authors: B.Ross,M.Gajhede,O.Kristensen
Key ref: B.Ross et al. (2007). High resolution crystal structures of the p120 RasGAP SH3 domain. Biochem Biophys Res Commun, 353, 463-468. PubMed id: 17188236 DOI: 10.1016/j.bbrc.2006.12.044
Date:
01-Aug-06     Release date:   02-Jan-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P20936  (RASA1_HUMAN) -  Ras GTPase-activating protein 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1047 a.a.
64 a.a.*
Protein chain
Pfam   ArchSchema ?
P20936  (RASA1_HUMAN) -  Ras GTPase-activating protein 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1047 a.a.
60 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     negative regulation of Ras protein signal transduction   2 terms 
  Biochemical function     Ras GTPase activator activity     1 term  

 

 
DOI no: 10.1016/j.bbrc.2006.12.044 Biochem Biophys Res Commun 353:463-468 (2007)
PubMed id: 17188236  
 
 
High resolution crystal structures of the p120 RasGAP SH3 domain.
B.Ross, O.Kristensen, D.Favre, J.Walicki, J.S.Kastrup, C.Widmann, M.Gajhede.
 
  ABSTRACT  
 
X-ray structures of two crystal forms of the Src homology 3 domain (SH3) of the Ras GTPase activating protein (RasGAP) were determined at 1.5 and 1.8A resolution. The overall structure comprises a single domain with two tightly packed beta-sheets linked by a short helical segment. An important motif for peptide binding in other SH3 domains is not conserved in RasGAP. The RasGAP SH3 domain forms dimers in the crystal structures, which may provide new functional insight. The dimer interface involves residues also present in a peptide previously identified as an apoptotic sensitizer of tumor cells.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19151751 X.Y.Yang, M.Guan, D.Vigil, C.J.Der, D.R.Lowy, and N.C.Popescu (2009).
p120Ras-GAP binds the DLC1 Rho-GAP tumor suppressor protein and inhibits its RhoA GTPase and growth-suppressing activities.
  Oncogene, 28, 1401-1409.  
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