2AFJ

SPRY domain-containing SOCS box protein 2 (SSB-2)


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 194 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with acceptable covalent geometry 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The SPRY domain of SSB-2 adopts a novel fold that presents conserved Par-4-binding residues

Masters, S.L.Yao, S.Willson, T.A.Zhang, J.G.Palmer, K.R.Smith, B.J.Babon, J.J.Nicola, N.A.Norton, R.S.Nicholson, S.E.

(2006) Nat Struct Mol Biol 13: 77-84

  • DOI: https://doi.org/10.1038/nsmb1034
  • Primary Citation of Related Structures:  
    2AFJ

  • PubMed Abstract: 

    The four mammalian SPRY domain-containing SOCS box proteins (SSB-1 to SSB-4) are characterized by a C-terminal SOCS box and a central SPRY domain. We have determined the first SPRY-domain structure, as part of SSB-2, by NMR. This domain adopts a novel fold consisting of a beta-sandwich structure formed by two four-stranded antiparallel beta-sheets with a unique topology. We demonstrate that SSB-1, SSB-2 and SSB-4, but not SSB-3, bind prostate apoptosis response protein-4 (Par-4). Mutational analysis of SSB-2 loop regions identified conserved structural determinants for its interaction with Par-4 and the hepatocyte growth factor receptor, c-Met. Mutations in analogous loop regions of pyrin and midline-1 SPRY domains have been shown to cause Mediterranean fever and Opitz syndrome, respectively. Our findings provide a template for SPRY-domain structure and an insight into the mechanism of SPRY-protein interaction.


  • Organizational Affiliation

    The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, 3050, Victoria, Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
gene rich cluster, C9 gene226Mus musculusMutation(s): 0 
Gene Names: Ssb-2
UniProt
Find proteins for O88838 (Mus musculus)
Explore O88838 
Go to UniProtKB:  O88838
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO88838
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 194 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with acceptable covalent geometry 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-01-03
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-09
    Changes: Data collection, Database references, Derived calculations