Structural and functional relationships of heterotrimeric G-proteins.
Heterotrimeric GTP-binding proteins (G-proteins) are a critical component of signal transduction pathways that carry information received at the cell surface to the appropriate cellular effector system, ultimately achieving a specific cellular response. Heterotrimeric G-proteins consist of an alpha-subunit, which contains the guanine nucleotide binding site and intrinsic GTPase activity, and an inseparable beta gamma-subunit complex. G-proteins act to define the specificity by which a receptor regulates a particular intracellular signaling system, as well as to regulate the duration of the signal. A great deal of structural and functional insight into how G-protein-mediated signal transduction occurs has recently been achieved. This review will discuss the structural features of G-proteins, as well as detail the mechanism by which G-proteins interact with receptors and effectors.
Rens-Domiano
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Department of Physiology and Biophysics, University of Illinois at Chicago, College of Medicine 60612, USA.
Hamm
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D019204:GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism; D015398:Signal Transduction; D013329:Structure-Activity Relationship
D011956:Receptors, Cell Surface; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins