4NJ8

Crystal structure of the human ANKS3 SAM Domain L52A mutant


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.200 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3.

Leettola, C.N.Knight, M.J.Cascio, D.Hoffman, S.Bowie, J.U.

(2014) BMC Struct Biol 14: 17-17

  • DOI: https://doi.org/10.1186/1472-6807-14-17
  • Primary Citation of Related Structures:  
    4NJ8, 4NL9

  • PubMed Abstract: 

    Autosomal dominant polycystic kidney disease (ADPKD) is the most common genetic disorder leading to end-stage renal failure in humans. In the PKD/Mhm(cy/+) rat model of ADPKD, the point mutation R823W in the sterile alpha motif (SAM) domain of the protein ANKS6 is responsible for disease. SAM domains are known protein-protein interaction domains, capable of binding each other to form polymers and heterodimers. Despite its physiological importance, little is known about the function of ANKS6 and how the R823W point mutation leads to PKD. Recent work has revealed that ANKS6 interacts with a related protein called ANKS3. Both ANKS6 and ANKS3 have a similar domain structure, with ankyrin repeats at the N-terminus and a SAM domain at the C-terminus.


  • Organizational Affiliation

    Department of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, Boyer Hall 611 Charles E, Young Dr, E, Los Angeles, California 90095-1570, USA. bowie@mbi.ucla.edu.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ankyrin repeat and SAM domain-containing protein 3
A, B
71Homo sapiensMutation(s): 1 
Gene Names: ANKS3KIAA1977
UniProt & NIH Common Fund Data Resources
Find proteins for Q6ZW76 (Homo sapiens)
Explore Q6ZW76 
Go to UniProtKB:  Q6ZW76
PHAROS:  Q6ZW76
GTEx:  ENSG00000168096 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6ZW76
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.200 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 71.89α = 90
b = 71.89β = 90
c = 33.54γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
XSCALEdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-07-16
    Type: Initial release
  • Version 1.1: 2019-07-17
    Changes: Data collection, Refinement description
  • Version 1.2: 2024-02-28
    Changes: Data collection, Database references