Protein:protein interactions in the lipid bilayer (review).
At least four different types of interaction between protein transmembrane helices have been described to date. These include the use of charge-pair interactions that can play a positive or negative role in the assembly of multi-subunit complexes such as the T cell receptor, or recruit signal transducing accessory molecules in the case of some Fc receptors. Inter-helix hydrogen bonds have been shown to play an important role in the constitutive activation of certain proto-oncogenes, whereas helix:helix interfaces stabilized solely by van der Waals contacts mediated by non-polar residues also exist. The fourth type of interaction is an inter-chain disulphide linkage which is dependent on a buried charged residue. A role for glycine residues in several of these mechanisms is also suggested. In addition, the use of disulphide mapping to further explore protein:protein interactions within the lipid bilayer is discussed.
Harrison
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Division of Biochemistry and Molecular Biology, University of Glasgow, UK.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D002628:Chemoreceptor Cells; D017124:Conserved Sequence; D004220:Disulfides / Q000737:chemistry; D004735:Energy Transfer; D029968:Escherichia coli Proteins; D006801:Humans; D008051:Lipid Bilayers; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D051381:Rats; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry / Q000378:metabolism; D011956:Receptors, Cell Surface; D017455:Receptors, IgE / Q000737:chemistry / Q000378:metabolism; D011971:Receptors, Immunologic / Q000737:chemistry / Q000378:metabolism; D054340:Receptors, KIR; D011990:Receptors, Transferrin / Q000737:chemistry / Q000378:metabolism; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism
D000596:Amino Acids; D001426:Bacterial Proteins; D004220:Disulfides; D029968:Escherichia coli Proteins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D011506:Proteins; D011948:Receptors, Antigen, T-Cell; D011956:Receptors, Cell Surface; D017455:Receptors, IgE; D011971:Receptors, Immunologic; D054340:Receptors, KIR; D011990:Receptors, Transferrin; C057331:Tar protein, E coli; C041476:Trg protein, E coli; D012697:Serine Endopeptidases; C026515:type I signal peptidase