Influence of solubilizing environments on membrane protein structures

Trends Biochem Sci. 2011 Feb;36(2):117-25. doi: 10.1016/j.tibs.2010.07.005. Epub 2010 Aug 18.

Abstract

Membrane protein structures are stabilized by weak interactions and are influenced by additional interactions with the solubilizing environment. Structures of influenza virus A M2 protein, a proven drug target, have been determined in three different environments, thus providing a unique opportunity to assess environmental influences. Structures determined in detergents and detergent micelles can have notable differences from those determined in lipid bilayers. These differences make it imperative to validate membrane protein structures.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Detergents / metabolism
  • Humans
  • Influenza A virus / chemistry
  • Ion Channels / chemistry
  • Ion Channels / metabolism
  • Lipid Bilayers
  • Membrane Proteins / chemistry*
  • Micelles
  • Models, Molecular
  • Viral Matrix Proteins / chemistry*
  • Viral Matrix Proteins / metabolism

Substances

  • Detergents
  • Ion Channels
  • Lipid Bilayers
  • M2 protein, Influenza A virus
  • Membrane Proteins
  • Micelles
  • Viral Matrix Proteins