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GTP-dependent protein binding

Definition

Target type: molecularfunction

Binding to a protein or protein complex when at least one of the interacting partners is in the GTP-bound state. [GOC:go_curators, GOC:krc]

GTP-dependent protein binding is a molecular function that involves the specific interaction of a protein with a guanosine triphosphate (GTP) molecule. GTP is a nucleotide that plays a crucial role in many cellular processes, including signal transduction, protein synthesis, and cytoskeletal dynamics. When GTP binds to a protein, it often induces conformational changes that can activate or inactivate the protein, altering its activity and function. This interaction is highly specific, with proteins possessing distinct GTP-binding domains that recognize and bind to GTP with high affinity. These domains typically consist of conserved amino acid sequences that form a pocket-like structure to accommodate the GTP molecule. The binding of GTP is often regulated by other factors, such as the presence of other proteins or small molecules, ensuring that the interaction occurs only when and where it is required. This dynamic interplay between GTP and proteins is essential for maintaining cellular homeostasis and responding to environmental cues. For instance, GTP-dependent protein binding is crucial for regulating the activity of signaling proteins, such as G-proteins, which are involved in transmitting signals from cell surface receptors to intracellular pathways. Additionally, GTP-binding proteins play vital roles in protein synthesis by facilitating the interaction between ribosomes and messenger RNA. Overall, GTP-dependent protein binding is a fundamental molecular mechanism that governs a wide range of cellular processes, underscoring its importance in maintaining cellular function and responding to environmental stimuli.'
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Proteins (1)

ProteinDefinitionTaxonomy
Cell division control protein 42 homologA cell division control protein 42 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P60953]Homo sapiens (human)

Compounds (7)

CompoundDefinitionClassesRoles
fasudilfasudil : An isoquinoline substituted by a (1,4-diazepan-1-yl)sulfonyl group at position 5. It is a Rho-kinase inhibitor and its hydrochloride hydrate form is approved for the treatment of cerebral vasospasm and cerebral ischemia.

fasudil: intracellular calcium antagonist; structure in first source
isoquinolines;
N-sulfonyldiazepane
antihypertensive agent;
calcium channel blocker;
EC 2.7.11.1 (non-specific serine/threonine protein kinase) inhibitor;
geroprotector;
neuroprotective agent;
nootropic agent;
vasodilator agent
ketorolac5-benzoyl-2,3-dihydro-1H-pyrrolizine-1-carboxylic acid : A member of the class of pyrrolizines that is 2,3-dihydro-1H-pyrrolizine which is substituted at positions 1 and 5 by carboxy and benzoyl groups, respectively.

ketorolac : A racemate comprising equimolar amounts of (R)-(+)- and (S)-(-)-5-benzoyl-2,3-dihydro-1H-pyrrolizine-1-carboxylic acid. While only the (S)-(-) enantiomer is a COX1 and COX2 inhibitor, the (R)-(+) enantiomer exhibits potent analgesic activity. A non-steroidal anti-inflammatory drug, ketorolac is mainly used (generally as the tromethamine salt) for its potent analgesic properties in the short-term management of post-operative pain, and in eye drops to relieve the ocular itching associated with seasonal allergic conjunctivitis. It was withdrawn from the market in many countries in 1993 following association with haemorrhage and renal failure.

Ketorolac: A pyrrolizine carboxylic acid derivative structurally related to INDOMETHACIN. It is an NSAID and is used principally for its analgesic activity. (From Martindale The Extra Pharmacopoeia, 31st ed)
amino acid;
aromatic ketone;
monocarboxylic acid;
pyrrolizines;
racemate
analgesic;
cyclooxygenase 1 inhibitor;
cyclooxygenase 2 inhibitor;
non-steroidal anti-inflammatory drug
sanguinarine chloride
chelerythrine chloride
2-[[benzamido(sulfanylidene)methyl]amino]-5,5-dimethyl-4,7-dihydrothieno[2,3-c]pyran-3-carboxylic acidCID1067700: a pan-GTPase inhibitor; structure in first sourcethienopyran
y 27632, dihydrochloride, (4(r)-trans)-isomer
secramine asecramine A: inhibits VSVG transport from the Golgi to the plasma membrane; also inhibits Cdc42-dependent cell functions; structure in first source