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Dostupne proteinske strukture:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Regulator G protein signalnog domena
Regulator G protein signalnog domena
	Struktura aktivnih konformacija Gi alfa 1.
Identifikatori
Simbol	RGS
Pfam	PF00615
InterPro	IPR000342
SMART	RGS
PROSITE	PDOC50132
SCOP	1gia
SUPERFAMILY	1gia
OPM protein	2bcj
Pfam
Dostupne proteinske strukture:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Regulatori G protein signalizacije (ili RGS) su proteinski strukturni domeni koji aktiviraju GTPaze za heterotrimerne G-proteinske alfa-podjedinice.

RGS proteini su multi-funkcionalni, ubrzavajući proteini GTPaza, koji podstiču GTP hidrolizu alfa podjedinicama heterotrimernih G proteina, čime inaktiviraju G protein i brzo prekidaju signalni puteve G protein-spregnutih receptora^[2]. Nakon aktivacije GPCR receptora, heterotrimerni G proteini razmenjuju GDP za GTP, odvajaju se od receptora, i disociraju se u slobodnu, aktivnu GTP-vezanu alfa podjedinicu i beta-gama dimer, ova od kojih aktiviraju nizvodne efektore. Respons se okončava nakon GTP hidrolize alfa podjedinice (IPR001019), koja se zatim vezuje sa beta-gama dimerom (IPR001632 IPR001770) i receptorom. RGS proteini primetno umanjuju životni vek GTP-vezanih alfa podjedinica i stabilizuju G protein prelazno stanje.

Primeri

Sledeći ljudski proteini sadrže ovaj domen:

ADRBK1, ADRBK2, AXIN1, AXIN2
GRK1, GRK4, GRK5, GRK6, GRK7,
RGS1, RGS2, RGS3, RGS4, RGS5, RGS6, RGS7, RGS8, RGS9, RGS10, RGS11, RGS12, RGS13, RGS14, RGS16, RGS17, RGS18, RGS19, RGS20, RGS21
RK
SNX13

Vidi još

GEF
GAP

Literatura

^ Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR (1994). „Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis”. Science. 265 (5177): 1405—12. PMID 8073283. doi:10.1126/science.8073283.
^ De Vries L, Farquhar MG, Zheng B, Fischer T, Elenko E (2000). „The regulator of G protein signaling family”. Annu. Rev. Pharmacol. Toxicol. 40: 235—271. PMID 10836135. doi:10.1146/annurev.pharmtox.40.1.235.

Dodatna literatura

Structure of RGS4 bound to AlF4—activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. Tesmer JJ, Berman DM, Gilman AG, Sprang SR; Cell 1997;89:251-261.
Tesmer JJ, Berman DM, Gilman AG, Sprang SR (1997). „Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis”. Cell. 89 (2): 251—61. PMID 9108480.
Dohlman HG, Apaniesk D, Chen Y, Song J, Nusskern D (1995). „Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae”. Mol. Cell. Biol. 15 (7): 3635—43. PMC 230601 . PMID 7791771.
Watson N, Linder ME, Druey KM, Kehrl JH, Blumer KJ (1996). „RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits”. Nature. 383 (6596): 172—5. PMID 8774882. doi:10.1038/383172a0.
Berman DM, Wilkie TM, Gilman AG (1996). „GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits”. Cell. 86 (3): 445—52. PMID 8756726.
De Vries L, Mousli M, Wurmser A, Farquhar MG (1995). „GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain”. Proc. Natl. Acad. Sci. U.S.A. 92 (25): 11916—20. PMC 40514 . PMID 8524874. doi:10.1073/pnas.92.25.11916.
Dohlman HG (2009). „RGS proteins: The early days”. Prog Mol Biol Transl Sci. 86: 1—14. PMID 20374711.

Spoljašnje veze

RGS domen^{[мртва веза]}

[pmid8073283-1] Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR (1994). „Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis”. Science. 265 (5177): 1405—12. PMID 8073283. doi:10.1126/science.8073283.

[PUB00006536-2] De Vries L, Farquhar MG, Zheng B, Fischer T, Elenko E (2000). „The regulator of G protein signaling family”. Annu. Rev. Pharmacol. Toxicol. 40: 235—271. PMID 10836135. doi:10.1146/annurev.pharmtox.40.1.235.

[1]

[2]

Regulator G protein signalizacije

Primeri

Vidi još

Literatura

Dodatna literatura

Spoljašnje veze