Structural aspects of oligomerization taking place between the transmembrane alpha-helices of bitopic membrane proteins.
Recent advances in biophysical methods have been able to shed more light on the structures of helical bundles formed by the transmembrane segments of bitopic membrane proteins. In this manuscript, I attempt to review the biological importance and diversity of these interactions, the energetics of bundle formation, motifs capable of inducing oligomerization and methods capable of detecting, solving and predicting the structures of these oligomeric bundles. Finally, the structures of the best characterized instances of transmembrane alpha-helical bundles formed by bitopic membrane proteins are described in detail.
Arkin
Isaiah T
IT
Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Givat-Ram, Jerusalem, Israel. arkin@cc.huji.ac.il
D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D019281:Dimerization; D019277:Entropy; D006021:Glycophorins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007473:Ion Channels / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D012399:Rotation; D017550:Spectroscopy, Fourier Transform Infrared; D040681:Structural Homology, Protein; D014763:Viral Matrix Proteins / Q000737:chemistry / Q000378:metabolism; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D006021:Glycophorins; D007473:Ion Channels; D008051:Lipid Bilayers; D008565:Membrane Proteins; D014763:Viral Matrix Proteins; D000099211:Phospholamban; C031540:M-protein, influenza virus