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Guanosine 5’-diphosphate GDP

The activated receptor combines with the G-protein in its Ggdp form, with the consequence that guanosine triphosphate (GTP) can replace previously bound guanosine diphosphate (GDP). The extent to which this can occur will be influenced by the local concentration of GTP. [Pg.32]

The most common second messenger activated by protein/peptide hormones and catecholamines is cyclic adenosine monophosphate (cAMP). The pathway by which cAMP is formed and alters cellular function is illustrated in Figure 10.1. The process begins when the hormone binds to its receptor. These receptors are quite large and span the plasma membrane. On the cytoplasmic surface of the membrane, the receptor is associated with a G protein that serves as the transducer molecule. In other words, the G protein acts as an intermediary between the receptor and the second messengers that will alter cellular activity. These proteins are referred to as G proteins because they bind with guanosine nucleotides. In an unstimulated cell, the inactive G protein binds guanosine diphosphate (GDP). When the hormone... [Pg.116]

G proteins comprise several families of diverse cellular proteins that subserve an equally diverse array of cellular functions. These proteins derive their name from the fact that they bind the guanine nucleotides guanosine triphosphate (GTP) and guanosine diphosphate (GDP) and possess intrinsic GTPase activity. G proteins play a central role in signal transduction as well as in a myriad of cellular processes, including membrane vesicle transport,... [Pg.335]

Guanine Guanosine GuanyUc acid Guanosine monophosphate (GMP) Guanosine diphosphate (GDP) Guanosine triphosphate (GTP)... [Pg.6]

There are several intracellular second messengers that are activated by metabotropic receptors, also referred to as G protein-coupled receptors (Duman and Nestler 1999). These receptors couple with G proteins that are heterotrimers made up of a-, (3- and y-subunits. Interaction of the G protein heterotrimer with activated receptor increases the exchange of guanosine triphosphate (GTP) for bound guanosine diphosphate (GDP), resulting in dissociation of the heterotrimer into free a and (3y subunits that in turn can regulate second messen-... [Pg.307]

As their name suggests, GPCRs bind G-proteins. A complete G-protein is a heterotri-mer of three separate proteins, consisting of a-, /3-, and -y-subunits. The a-subunit binds either guanosine diphosphate (GDP) or triphosphate (GTP). The affinity for GDP/GTP is the origin of the name G-protein. The G-protein heterotrimer binds GPCRs on both the C-terminal tail and the linker between the fifth and sixth transmembrane helices on the intracellular face of the receptor.12... [Pg.98]

STEPS s-6 Hydrolysis and dehydrogenation of succinyl CoA. Succinyl CoA is hydrolyzed to succinate in step 5. The reaction is catalyzed by succinyl CoA synthetase and is coupled with phosphorylation of guanosine diphosphate (GDP) to give guanosine triphosphate (GTP). The overall transformation is similar to that of step 8 in glycolysis (Figure 29.4), in which a thiol ester is converted into an acyl phosphate and a phosphate group is then transferred to ADP. [Pg.1215]


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