1HO7

NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 
  • Selection Criteria: closest to average structure 

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This is version 1.3 of the entry. See complete history


Literature

Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel.

Ohlenschlager, O.Hojo, H.Ramachandran, R.Gorlach, M.Haris, P.I.

(2002) Biophys J 82: 2995-3002

  • DOI: https://doi.org/10.1016/S0006-3495(02)75640-3
  • Primary Citation of Related Structures:  
    1HO2, 1HO7

  • PubMed Abstract: 

    The propagation of action potentials during neuronal signal transduction in phospholipid membranes is mediated by ion channels, a diverse group of membrane proteins. The S4-S5 linker peptide (S4-S5), that connects the S4 and S5 transmembrane segments of voltage-gated potassium channels is an important region of the Shaker ion-channel protein. Despite its importance, very little is known about its structure. Here we provide evidence for an amphipathic alpha-helical conformation of a synthetic S4-S5 peptide of the voltage-gated Drosophila melanogaster Shaker potassium channel in water/trifluoroethanol and in aqueous phospholipid micelles. The three-dimensional solution structures of the S4-S5 peptide were obtained by high-resolution nuclear magnetic resonance spectroscopy and distance-geometry/simulated-annealing calculations. The detailed structural features are discussed with respect to model studies and available mutagenesis data on the mechanism and selectivity of the potassium channel.


  • Organizational Affiliation

    Institut für Molekulare Biotechnologie, Centre for Design and Structure in Biology, D-07708 Jena, Germany.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN20Drosophila melanogasterMutation(s): 0 
UniProt
Find proteins for P08510 (Drosophila melanogaster)
Explore P08510 
Go to UniProtKB:  P08510
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08510
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 
  • Selection Criteria: closest to average structure 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-06-05
    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: 2022-02-23
    Changes: Database references, Derived calculations