Structural heterogeneity of membrane receptors and GTP-binding proteins and its functional consequences for signal transduction.
Recent information obtained, mainly by recombinant cDNA technology, on structural heterogeneity of hormone and transmitter receptors, of GTP-binding proteins (G-proteins) and, especially, of G-protein-linked receptors is reviewed and the implications of structural heterogeneity for diversity of hormone and transmitter actions is discussed. For the future, three-dimensional structural analysis of membrane proteins participating in signal transmission and transduction pathways is needed in order to understand the molecular basis of allosteric regulatory mechanisms governing the interactions between these proteins including hysteretic properties and cell-cybernetic aspects.
Boege
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F
Department of Physiological Chemistry, University of Würzburg, Federal Republic of Germany.
Neumann
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E
Helmreich
E J
EJ
D000109:Acetylcholine / Q000378:metabolism; D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D011487:Protein Conformation; D011942:Receptors, Adrenergic, alpha / Q000378:metabolism; D015398:Signal Transduction; D014422:Turkeys
D008565:Membrane Proteins; D011942:Receptors, Adrenergic, alpha; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases; D000109:Acetylcholine