1UJL

Solution Structure of the HERG K+ channel S5-P extracellular linker


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 1600 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of the HERG K+ channel S5P extracellular linker: role of an amphipathic alpha-helix in C-type inactivation.

Torres, A.M.Bansal, P.S.Sunde, M.Clarke, C.E.Bursill, J.A.Smith, D.J.Bauskin, A.Breit, S.N.Campbell, T.J.Alewood, P.F.Kuchel, P.W.Vandenberg, J.I.

(2003) J Biol Chem 278: 42136-42148

  • DOI: https://doi.org/10.1007/s00249-003-0338-3
  • Primary Citation of Related Structures:  
    1UJL

  • PubMed Abstract: 

    The HERG K+ channel has very unusual kinetic behaviour that includes slow activation but rapid inactivation. These features are critical for normal cardiac repolarisation as well as in preventing lethal ventricular arrhythmias. Extensive mutagenesis of the HERG K+ channel has allowed identification of which regions of the channel are important for the unusual kinetic behaviour of the channel. Furthermore, structural studies on scorpion toxins that potently inhibit HERG are beginning to provide clues as to the structural differences between HERG and other voltage-gated K+ channels.


  • Organizational Affiliation

    Victor Chang Cardiac Research Institute, Level 9, 384 Victoria Street, Darlinghurst, NSW, 2010, Australia. j.vandenberg@victorchang.unsw.edu.au


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Potassium voltage-gated channel subfamily H member 242N/AMutation(s): 0 
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for Q12809 (Homo sapiens)
Explore Q12809 
Go to UniProtKB:  Q12809
PHAROS:  Q12809
GTEx:  ENSG00000055118 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ12809
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 1600 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2003-11-04
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2023-12-27
    Changes: Data collection