3JXI

Crystal structure of the chicken TRPV4 ankyrin repeat domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.204 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C.

Landoure, G.Zdebik, A.A.Martinez, T.L.Burnett, B.G.Stanescu, H.C.Inada, H.Shi, Y.Taye, A.A.Kong, L.Munns, C.H.Choo, S.S.Phelps, C.B.Paudel, R.Houlden, H.Ludlow, C.L.Caterina, M.J.Gaudet, R.Kleta, R.Fischbeck, K.H.Sumner, C.J.

(2010) Nat Genet 42: 170-174

  • DOI: https://doi.org/10.1038/ng.512
  • Primary Citation of Related Structures:  
    3JXI, 3JXJ

  • PubMed Abstract: 

    Charcot-Marie-Tooth disease type 2C (CMT2C) is an autosomal dominant neuropathy characterized by limb, diaphragm and laryngeal muscle weakness. Two unrelated families with CMT2C showed significant linkage to chromosome 12q24.11. We sequenced all genes in this region and identified two heterozygous missense mutations in the TRPV4 gene, C805T and G806A, resulting in the amino acid substitutions R269C and R269H. TRPV4 is a well-known member of the TRP superfamily of cation channels. In TRPV4-transfected cells, the CMT2C mutations caused marked cellular toxicity and increased constitutive and activated channel currents. Mutations in TRPV4 were previously associated with skeletal dysplasias. Our findings indicate that TRPV4 mutations can also cause a degenerative disorder of the peripheral nerves. The CMT2C-associated mutations lie in a distinct region of the TRPV4 ankyrin repeats, suggesting that this phenotypic variability may be due to differential effects on regulatory protein-protein interactions.


  • Organizational Affiliation

    Department of Medicine, University College London, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Vanilloid receptor-related osmotically activated channel protein
A, B, C, D
260Gallus gallusMutation(s): 0 
Gene Names: TRPV4VR-OAC
UniProt
Find proteins for A0A1D5PXA5 (Gallus gallus)
Explore A0A1D5PXA5 
Go to UniProtKB:  A0A1D5PXA5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1D5PXA5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.204 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 105.259α = 90
b = 48.119β = 101.89
c = 133.891γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
CrystalCleardata collection
HKL-2000data reduction
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-12-22
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2017-11-01
    Changes: Refinement description
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Refinement description