3EAC

Crystal structure of SH2 domain of Human Csk (carboxyl-terminal src kinase), Oxidized form.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.37 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.209 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.

Liu, D.Cowburn, D.

(2016) Biophys Rep 2: 33-43

  • DOI: https://doi.org/10.1007/s41048-016-0025-4
  • Primary Citation of Related Structures:  
    3EAC, 3EAZ

  • PubMed Abstract: 

    The Src Homology 2 (SH2) domain is a structurally conserved protein domain that typically binds to a phosphorylated tyrosine in a peptide motif from the target protein. The SH2 domain of C-terminal Src kinase (Csk) contains a single disulfide bond, which is unusual for most SH2 domains. Although the global motion of SH2 domain regulates Csk function, little is known about the relationship between the disulfide bond and binding of the ligand. In this study, we combined X-ray crystallography, solution NMR, and other biophysical methods to reveal the interaction network in Csk. Denaturation studies have shown that disulfide bond contributes significantly to the stability of SH2 domain, and crystal structures of the oxidized and C122S mutant showed minor conformational changes. We further investigated the binding of SH2 domain to a phosphorylated peptide from Csk-binding protein upon reduction and oxidation using both NMR and fluorescence approaches. This work employed NMR, X-ray cryptography, and other biophysical methods to study a disulfide bond in Csk SH2 domain. In addition, this work provides in-depth understanding of the structural dynamics of Csk SH2 domain.


  • Organizational Affiliation

    iHuman Institute, ShanghaiTech University, Shanghai, 201203 China ; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461 USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tyrosine-protein kinase CSK106Homo sapiensMutation(s): 0 
Gene Names: CSK
EC: 2.7.10.2
UniProt & NIH Common Fund Data Resources
Find proteins for P41240 (Homo sapiens)
Explore P41240 
Go to UniProtKB:  P41240
PHAROS:  P41240
GTEx:  ENSG00000103653 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP41240
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.37 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.209 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37.114α = 90
b = 48.025β = 90
c = 49.866γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MAR345dtbdata collection
HKL-2000data reduction
HKL-2000data scaling
AMoREphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-11-10
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2014-12-10
    Changes: Version format compliance
  • Version 1.3: 2016-07-20
    Changes: Database references
  • Version 1.4: 2016-12-14
    Changes: Database references
  • Version 1.5: 2023-08-30
    Changes: Data collection, Database references, Refinement description