Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies

J Struct Biol. 2007 Dec;160(3):265-74. doi: 10.1016/j.jsb.2007.07.001. Epub 2007 Jul 14.

Abstract

The recombinant expression of eukaryotic membrane proteins has been a major stumbling block in efforts to determine their structures. In the last two years, however, five such proteins have yielded high-resolution X-ray or electron diffraction data, opening the prospect of increased throughput for eukaryotic membrane protein structure determination. Here, we summarize the major expression systems available, and highlight technical advances that should facilitate more systematic screening of expression conditions for this physiologically important class of targets.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Baculoviridae / genetics
  • Cell Line
  • Chromatography, Affinity
  • Cloning, Molecular / methods*
  • Crystallography / methods*
  • Crystallography, X-Ray
  • Escherichia coli
  • Genetic Vectors / genetics
  • Humans
  • Insecta / cytology
  • Mammals
  • Membrane Proteins / biosynthesis*
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Microscopy, Electron, Transmission / methods*
  • Molecular Chaperones / physiology
  • Multiprotein Complexes
  • Protein Conformation*
  • Recombinant Fusion Proteins / biosynthesis*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / isolation & purification
  • Transfection / methods
  • Yeasts

Substances

  • Membrane Proteins
  • Molecular Chaperones
  • Multiprotein Complexes
  • Recombinant Fusion Proteins