1H3H

Structural Basis for Specific Recognition of an RxxK-containing SLP-76 peptide by the Gads C-terminal SH3 domain


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: LOWEST ENERGY 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structural Basis for Specific Binding of the Gads SH3 Domain to an Rxxk Motif-Containing Slp-76 Peptide: A Novel Mode of Peptide Recognition

Liu, Q.Berry, D.Nash, P.Pawson, T.Mcglade, C.J.Li, S.S.

(2003) Mol Cell 11: 471

  • DOI: https://doi.org/10.1016/s1097-2765(03)00046-7
  • Primary Citation of Related Structures:  
    1H3H

  • PubMed Abstract: 

    The SH3 domain, which normally recognizes proline-rich sequences, has the potential to bind motifs with an RxxK consensus. To explore this novel specificity, we have determined the solution structure of the Gads T cell adaptor C-terminal SH3 domain in complex with an RSTK-containing peptide, representing its physiological binding site on the SLP-76 docking protein. The SLP-76 peptide engages four distinct binding pockets on the surface of the Gads SH3 domain and upon binding adopts a unique structure characterized by a right-handed 3(10) helix at the RSTK locus, in contrast to the left-handed polyproline type II helix formed by canonical proline-rich SH3 ligands. The structure, and supporting mutagenesis and peptide binding data, reveal a novel mode of ligand recognition by SH3 domains.


  • Organizational Affiliation

    Department of Biochemistry, Faculty of Medicine and Dentistry, University of Western Ontario, N6A 5C1, London, Ontario, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GRB2-RELATED ADAPTOR PROTEIN 260Mus musculusMutation(s): 0 
UniProt
Find proteins for O89100 (Mus musculus)
Explore O89100 
Go to UniProtKB:  O89100
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO89100
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
LYMPHOCYTE CYTOSOLIC PROTEIN 211Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q13094 (Homo sapiens)
Explore Q13094 
Go to UniProtKB:  Q13094
PHAROS:  Q13094
GTEx:  ENSG00000043462 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ13094
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: LOWEST ENERGY 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-03-06
    Type: Initial release
  • Version 1.1: 2013-07-24
    Changes: Derived calculations, Other, Source and taxonomy, Version format compliance