Literature DB >> 7524164

Using sequence homology to analyze the structure and function of voltage-gated ion channel proteins.

H R Guy1, S R Durell.   

Abstract

Molecular modeling and mutagenesis analysis of voltage-gated channels have succeeded in identifying much of the topology of the proteins and in identifying which sequential segments are involved in functional mechanisms such as activation gating, inactivation gating, ion selectivity, and ligand binding. Efforts are currently underway to use these methods to model the protein structure and functional mechanisms more precisely. The experimental and theoretical efforts are dependent to a considerable extent upon information obtained by comparing homologous sequences. Although the fine details of models developed in this manner are unlikely to be as correct as models developed from x-ray crystallography and NMR, they still may contribute substantially to our understanding of the structure and function of these important proteins.

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Year:  1994        PMID: 7524164

Source DB:  PubMed          Journal:  Soc Gen Physiol Ser        ISSN: 0094-7733


  6 in total

1.  Structural models of the KtrB, TrkH, and Trk1,2 symporters based on the structure of the KcsA K(+) channel.

Authors:  S R Durell; H R Guy
Journal:  Biophys J       Date:  1999-08       Impact factor: 4.033

2.  Structural models of the MscL gating mechanism.

Authors:  S Sukharev; S R Durell; H R Guy
Journal:  Biophys J       Date:  2001-08       Impact factor: 4.033

3.  A model of voltage gating developed using the KvAP channel crystal structure.

Authors:  Indira H Shrivastava; Stewart R Durell; H Robert Guy
Journal:  Biophys J       Date:  2004-10       Impact factor: 4.033

4.  Shaker pore structure as predicted by annealed atomic simulation using symmetry and novel geometric restraints.

Authors:  P K Yang; C Y Lee; M J Hwang
Journal:  Biophys J       Date:  1997-06       Impact factor: 4.033

5.  Orientation independence of single-vacancy and single-ion permeability ratios.

Authors:  P McGill; M F Schumaker
Journal:  Biophys J       Date:  1995-07       Impact factor: 4.033

6.  Unidirectional K+ fluxes through recombinant Shaker potassium channels expressed in single Xenopus oocytes.

Authors:  P Stampe; T Begenisich
Journal:  J Gen Physiol       Date:  1996-04       Impact factor: 4.086

  6 in total

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