1DXX

N-terminal Actin-binding Domain of Human Dystrophin

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.232 

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This is version 1.3 of the entry. See complete history. 


Literature

The Structure of the N-Terminal Actin-Binding Domain of Human Dystrophin and How Mutations in This Domain May Cause Duchenne or Becker Muscular Dystrophy

Norwood, F.L., Sutherland-Smith, A.J., Keep, N.H., Kendrick-Jones, J.

(2000) Structure 8: 481

  • DOI: https://doi.org/10.1016/s0969-2126(00)00132-5
  • Primary Citation of Related Structures:  
    1DXX

  • PubMed Abstract: 

    Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane. Dystrophin is therefore thought to serve as a link from the actin-based cytoskeleton of the muscle cell through the plasma membrane to the extracellular matrix. Pathogenic mutations in dystrophin result in Duchenne or Becker muscular dystrophy.

    • Organizational Affiliation: 

    Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, CB2 2QH, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DYSTROPHIN
A, B, C, D
246Homo sapiensMutation(s): 2 
Gene Names: DMD
UniProt & NIH Common Fund Data Resources
Find proteins for P11532 (Homo sapiens)
Explore P11532 
Go to UniProtKB:  P11532
PHAROS:  P11532
GTEx:  ENSG00000198947 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP11532
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.232 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.69α = 61.08
b = 79.33β = 78.22
c = 81.95γ = 70.54
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-05-16
    Type: Initial release
  • Version 1.1: 2011-05-07
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-06
    Changes: Data collection, Database references, Other, Refinement description