Search results
Results From The WOW.Com Content Network
Cyclic guanosine monophosphate (cGMP) is a cyclic nucleotide derived from guanosine triphosphate (GTP). cGMP acts as a second messenger much like cyclic AMP.Its most likely mechanism of action is activation of intracellular protein kinases in response to the binding of membrane-impermeable peptide hormones to the external cell surface. [1]
In response to calcium levels, guanylate cyclase synthesizes cGMP from GTP. cGMP keeps cGMP-gated channels open, allowing for the entry of calcium into the cell. [ 2 ] Like cAMP , cGMP is an important second messenger that internalizes the message carried by intercellular messengers such as peptide hormones and nitric oxide and can also ...
In mammalian cells, cGAMP is synthesized by cyclic GMP-AMP synthase from ATP and GTP upon cytosolic DNA stimulation. [2] cGAMP produced by cGAS contains mixed phosphodiester linkages, with one between 2'-OH of GMP and 5'-phosphate of AMP and the other between 3'-OH of AMP and 5'-phosphate of GMP. [3] [4] [5] [6]
Atrial natriuretic peptide (ANP) or atrial natriuretic factor (ANF) is a natriuretic peptide hormone secreted from the cardiac atria that in humans is encoded by the NPPA gene. [5] Natriuretic peptides (ANP, BNP , and CNP ) are a family of hormone/paracrine factors that are structurally related. [ 6 ]
The G s alpha subunit of the stimulated G protein complex exchanges GDP for GTP and is released from the complex. [4] In a cAMP-dependent pathway, the activated G s alpha subunit binds to and activates an enzyme called adenylyl cyclase, which, in turn, catalyzes the conversion of ATP into cyclic adenosine monophosphate (cAMP). [5]
GTP-binding protein regulators regulate G proteins in several different ways. Small GTPases act as molecular switches in signaling pathways, which act to regulate functions of other proteins. They are active or 'ON' when it is bound to GTP and inactive or 'OFF' when bound to GDP . [ 1 ]
Structurally, GBPs consist of two domains: a globular N- terminal domain harboring the GTPase function, and an extended C- terminal helical domain. [3] [5] In addition, some members of the GBPs family harbor motifs (e.g., CaaX motifs) or additional domains that are thought to operate in protein-protein or protein-membrane interactions.
Guanylyl transferases are enzymes that transfer a guanosine mono phosphate group, usually from GTP to another molecule, releasing pyrophosphate. Many eukaryotic guanylyl transferases are capping enzymes that catalyze the formation of the 5' cap in the co-transcriptional modification of messenger RNA .