3C5R

Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.202 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences.

Fox, D.Le Trong, I.Rajagopal, P.Brzovic, P.S.Stenkamp, R.E.Klevit, R.E.

(2008) J Biol Chem 283: 21179-21186

  • DOI: https://doi.org/10.1074/jbc.M802333200
  • Primary Citation of Related Structures:  
    3C5R

  • PubMed Abstract: 

    BARD1 is the constitutive nuclear partner to the breast and ovarian cancer-specific tumor suppressor BRCA1. Together, they form a heterodimeric complex responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. We report the 2.0A structure of the BARD1 ankyrin repeat domain. The structure includes four ankyrin repeats with a non-canonical C-terminal capping ankyrin repeat and a well ordered extended loop preceding the first repeat. Conserved surface features show an acidic patch and an acidic pocket along the surface typically used by ankyrin repeat domains for binding cognate proteins. We also demonstrate that two reported mutations, N470S and V507M, in the ankyrin repeat domain do not result in observable structural defects. These results provide a structural basis for exploring the biological function of the ankyrin repeat domain and for modeling BARD1 isoforms.


  • Organizational Affiliation

    Department of Biochemistry, University of Washington, Seattle, WA 98195-7350, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BRCA1-associated RING domain protein 1
A, B
137Homo sapiensMutation(s): 0 
Gene Names: BARD1
UniProt & NIH Common Fund Data Resources
Find proteins for Q99728 (Homo sapiens)
Explore Q99728 
Go to UniProtKB:  Q99728
PHAROS:  Q99728
GTEx:  ENSG00000138376 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ99728
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.202 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37.847α = 90
b = 74.112β = 105.23
c = 51.174γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
CrystalCleardata collection
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-05-13
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2023-08-30
    Changes: Data collection, Database references, Refinement description