European Biophysics Journal

, Volume 39, Issue 5, pp 723–755

Crystal structures of all-alpha type membrane proteins

  • Karen McLuskey
  • Aleksander W. Roszak
  • Yanshi Zhu
  • Neil W. Isaacs
Review

DOI: 10.1007/s00249-009-0546-6

Cite this article as:
McLuskey, K., Roszak, A.W., Zhu, Y. et al. Eur Biophys J (2010) 39: 723. doi:10.1007/s00249-009-0546-6

Abstract

Integral membrane proteins are involved in a wide range of essential biological functions and the determination of their three-dimensional structures plays a central role in understanding their function. This review focuses on the structures of one class of integral membrane proteins: the functionally diverse all-alpha type membrane proteins. It gives an overview of all the structures determined by X-ray crystallography, describing each system and structure in turn. It shows that the structures of all-alpha type membrane proteins have made valuable contributions to understanding structure–function relationships in membrane proteins. These range from the first insights into the function of exciting individual proteins to an in-depth knowledge of protein function from entire biological systems.

Keywords

Crystal structures All-alpha type membrane proteins X-ray crystallography 

Copyright information

© European Biophysical Societies' Association 2009

Authors and Affiliations

  • Karen McLuskey
    • 1
  • Aleksander W. Roszak
    • 1
  • Yanshi Zhu
    • 1
  • Neil W. Isaacs
    • 1
  1. 1.Westchem, Department of Chemistry, Glasgow Biomedical Research CentreUniversity of GlasgowGlasgowUK

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