Minimal art: or why small viral K(+) channels are good tools for understanding basic structure and function relations

Biochim Biophys Acta. 2011 Feb;1808(2):580-8. doi: 10.1016/j.bbamem.2010.04.008. Epub 2010 Apr 24.

Abstract

Some algal viruses contain genes that encode proteins with the hallmarks of K(+) channels. One feature of these proteins is that they are less than 100 amino acids in size, which make them truly minimal for a K(+) channel protein. That is, they consist of only the pore module present in more complex K(+) channels. The combination of miniature size and the functional robustness of the viral K(+) channels make them ideal model systems for studying how K(+) channels work. Here we summarize recent structure/function correlates from these channels, which provide insight into functional properties such as gating, pharmacology and sorting in cells.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • HEK293 Cells
  • Humans
  • Ion Channel Gating
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Molecular Sequence Data
  • Phycodnaviridae / chemistry
  • Phycodnaviridae / genetics
  • Phycodnaviridae / metabolism
  • Potassium Channels / chemistry*
  • Potassium Channels / genetics
  • Potassium Channels / metabolism*
  • Protein Structure, Quaternary
  • Sequence Homology, Amino Acid
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*

Substances

  • Kcv potassium channel, Chlorella virus
  • Potassium Channels
  • Viral Proteins