1XTE

crystal structure of CISK-PX domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX)

Xing, Y.Liu, D.Zhang, R.Joachimiak, A.Songyang, Z.Xu, W.

(2004) J Biol Chem 279: 30662-30669

  • DOI: https://doi.org/10.1074/jbc.M404107200
  • Primary Citation of Related Structures:  
    1XTE, 1XTN

  • PubMed Abstract: 

    The cytokine-independent survival kinase (CISK) in the serum and glucocorticoid-regulated kinase family plays an important role in mediating cell growth and survival. N-terminal to its catalytic kinase domain, CISK contains a phox homology (PX) domain, a phosphoinositide-binding motif that directs the membrane localization of CISK and regulates CISK activity. We have determined the crystal structures of the mouse CISK-PX domain to unravel the structural basis of membrane targeting of CISK. In addition to the specific interactions conferred by the phosphoinositide-binding pocket, the structure suggests that a hydrophobic loop region and a hydrophilic beta-turn contribute to the interactions with the membrane. Furthermore, biochemical studies reveal that CISK-PX dimerizes in the presence of the linker between the PX domain and kinase domain, suggesting a multivalent mechanism in membrane localization of CISK.


  • Organizational Affiliation

    Department of Biological Structure, University of Washington, Seattle, Washington 98195-7420, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase Sgk3154Mus musculusMutation(s): 0 
Gene Names: Cisk
EC: 2.7.1.37
UniProt
Find proteins for Q9ERE3 (Mus musculus)
Explore Q9ERE3 
Go to UniProtKB:  Q9ERE3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9ERE3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 74.954α = 90
b = 74.954β = 90
c = 51.697γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-11-16
    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: 2018-01-24
    Changes: Database references, Structure summary
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references