title: Crystal structures of all-alpha type membrane proteins.
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.
authors.affiliation: Westchem, Department of Chemistry, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA, UK. k.mcluskey@chem.gla.ac.uk
authors.forename: Karen
authors.initials: K
authors.lastname: McLuskey
authors.forename: Aleksander W
authors.initials: AW
authors.lastname: Roszak
authors.forename: Yanshi
authors.initials: Y
authors.lastname: Zhu
authors.forename: Neil W
authors.initials: NW
authors.lastname: Isaacs
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation
chemical_list: D008565:Membrane Proteins