1OJ5

Crystal structure of the Nco-A1 PAS-B domain bound to the STAT6 transactivation domain LXXLL motif


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.21 Å
  • R-Value Free: 0.214 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.170 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of the Ncoa-1/Src-1 Pas-B Domain Bound to the Lxxll Motif of the Stat6 Transactivation Domain

Razeto, A.Ramakrishnan, V.Litterst, C.M.Giller, K.Griesinger, C.Carlomagno, T.Lakomek, N.Heimburg, T.Lodrini, M.Pfitzner, E.Becker, S.

(2004) J Mol Biol 336: 319

  • DOI: https://doi.org/10.1016/j.jmb.2003.12.057
  • Primary Citation of Related Structures:  
    1OJ5

  • PubMed Abstract: 

    Signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 (IL-4) by direct interaction with coactivators. The CREB-binding protein (p300/CBP) and the nuclear coactivator 1 (NCoA-1), a member of the p160/steroid receptor coactivator family, bind independently to specific regions of the STAT6 transactivation domain and act as coactivators. The interaction between STAT6 and NCoA-1 is mediated by an LXXLL motif in the transactivation domain of STAT6. To define the mechanism of coactivator recognition, we determined the crystal structure of the NCoA-1 PAS-B domain in complex with the STAT6 LXXLL motif. The amphipathic, alpha-helical STAT6 LXXLL motif binds mostly through specific hydrophobic interactions to NCoA-1. A single amino acid of the NCoA-1 PAS-B domain establishes hydrophilic interactions with the STAT6 peptide. STAT6 interacts only with the PAS-B domain of NCoA-1 but not with the homologous regions of NCoA-2 and NCoA-3. The residues involved in binding the STAT6 peptide are strongly conserved between the different NCoA family members. Therefore surface complementarity between the hydrophobic faces of the STAT6 fragment and of the NCoA-1 PAS-B domain almost exclusively defines the binding specificity between the two proteins.


  • Organizational Affiliation

    Department for NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
STEROID RECEPTOR COACTIVATOR 1A132Mus musculusMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P70365 (Mus musculus)
Explore P70365 
Go to UniProtKB:  P70365
IMPC:  MGI:1276523
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP70365
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 614Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P42226 (Homo sapiens)
Explore P42226 
Go to UniProtKB:  P42226
PHAROS:  P42226
GTEx:  ENSG00000166888 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP42226
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.21 Å
  • R-Value Free: 0.214 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.170 
  • Space Group: P 62
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.1α = 90
b = 62.1β = 90
c = 73.4γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHELXDphasing
SHELXEphasing
REFMACrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-02-12
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance