3O5Z

Crystal structure of the SH3 domain from p85beta subunit of phosphoinositide 3-kinase (PI3K)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.01 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.216 

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This is version 1.2 of the entry. See complete history


Literature

X-ray structure of the SH3 domain of the phosphoinositide 3-kinase p85 beta subunit

Chen, S.Xiao, Y.Ponnusamy, R.Tan, J.Lei, J.Hilgenfeld, R.

(2011) Acta Crystallogr Sect F Struct Biol Cryst Commun 67: 1328-1333

  • DOI: https://doi.org/10.1107/S1744309111031691
  • Primary Citation of Related Structures:  
    3O5Z

  • PubMed Abstract: 

    Src-homology 3 (SH3) domains are involved in extensive protein-protein interactions and constitute key elements of intracellular signal transduction. Three-dimensional structures have been reported for SH3 domains of various proteins, including the 85 kDa regulatory subunit (p85) of phosphoinositide 3-kinase. However, all of the latter structures are of p85 isoform α and no crystal structure of the SH3 domain of the equally important isoform β has been reported to date. In this structural communication, the recombinant production, crystallization and X-ray structure determination at 2.0 Å resolution of the SH3 domain of human p85β is described. The structure reveals a compact β-barrel fold very similar to that of p85α. However, binding studies with two classes of proline-rich ligand peptides demonstrate that the ligand-binding specificity differs slightly between the SH3 domains of human p85β and p85α, despite their high structural similarity.


  • Organizational Affiliation

    Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Phosphatidylinositol 3-kinase regulatory subunit beta
A, B
90Homo sapiensMutation(s): 0 
Gene Names: PIK3R2
UniProt & NIH Common Fund Data Resources
Find proteins for O00459 (Homo sapiens)
Explore O00459 
Go to UniProtKB:  O00459
PHAROS:  O00459
GTEx:  ENSG00000105647 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO00459
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.01 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.216 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.01α = 90
b = 57.79β = 90
c = 62.97γ = 90
Software Package:
Software NamePurpose
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
DNAdata collection
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-08-10
    Type: Initial release
  • Version 1.1: 2011-11-09
    Changes: Database references
  • Version 1.2: 2014-09-10
    Changes: Database references