Stimulator of interferon genes - Revision history

Michal Harel at 07:29, 11 April 2022

Michal Harel — Mon, 11 Apr 2022 07:29:27 GMT

←Older revision		Revision as of 07:29, 11 April 2022
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	[[Stimulator of interferon genes protein 3D structures]]		[[Stimulator of interferon genes protein 3D structures]]
	</StructureSection>		</StructureSection>
-	==3D structures of stimulator of interferon genes protein==

-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-	*Stimulator of interferon genes protein; domains - C-di-GMP-binding 154-341; PLPLRT/SD motif 342-379
-
-	**[[6nt5]] – hSTING - human - Cryo EM<br />
-	**[[4ef5]], [[4f5w]], [[4f9e]] – hSTING C-di-GMP-binding domain<br />
-	**[[4f5e]], [[6mx0]] – hSTING C-di-GMP-binding domain (mutant)<br />
-	**[[6iyf]] – pSTING C-di-GMP-binding domain - pig<br />
-	**[[4kc0]] – mSTING C-di-GMP-binding domain - mouse<br />
-	**[[5gs5]] – rSTING C-di-GMP-binding domain - rat<br />
-	**[[6nt6]] – cSTING - chicken - Cryo EM<br />
-	**[[5cfo]], [[5cfr]] – aSTING – anemone<br />
-
-	*Stimulator of interferon genes protein complex
-
-	**[[4ef4]], [[4emt]], [[4emu]], [[4f5y]], [[4f9g]], [[6rm0]], [[6s86]] – hSTING C-di-GMP-binding domain + GMP derivative<br />
-	**[[4f5d]] – hSTING C-di-GMP-binding domain (mutant) + GMP derivative <br />
-	**[[6cff]], [[6cy7]] – hSTING C-di-GMP-binding domain + AMP derivative <br />
-	**[[4ksy]], [[4loh]], [[5bqx]], [[6dnk]], [[6xnp]], [[6s26]], [[6s27]] – hSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[4loi]], [[6mx3]], [[6mxe]] – hSTING C-di-GMP-binding domain (mutant) + GMP-AMP derivative <br />
-	**[[6dxg]], [[6dxl]], [[6ukm]], [[6uku]], [[6ukv]], [[6ukw]], [[6ukx]], [[6uky]], [[6ukz]], [[6ul0]] – hSTING C-di-GMP-binding domain + agonist <br />
-	**[[4qxo]] – hSTING C-di-GMP-binding domain + drug <br />
-	**[[4qxp]], [[4qxq]], [[4qxr]] – hSTING C-di-GMP-binding domain (mutant) + drug <br />
-	**[[5jej]] – hSTING PLPLRT/SD motif + IRF-3 CTD <br />
-	**[[6o8b]], [[6o8c]] – hSTING PLPLRT/SD motif (mutant) + TBK1 <br />
-	**[[6a03]], [[6a04]], [[6a05]], [[6a06]] – pSTING C-di-GMP-binding domain + ligand <br />
-	**[[4kby]] – mSTING C-di-GMP-binding domain+ GMP derivative<br />
-	**[[4loj]], [[4lok]], [[4yp1]] – mSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[6xnn]] – mSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[4lol]] – mSTING C-di-GMP-binding domain + drug <br />
-	**[[4jc5]] – mSTING C-di-GMP-binding domain + immune activator <br />
-	**[[5grm]] – rSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[6nt7]], [[6nt8]] – cSTING + GMP-AMP derivative - Cryo EM<br />
-	**[[6nt9]] – cSTING + TBK1 - Cryo EM<br />
-	**[[5cfl]], [[5cfm]], [[5cfq]] – aSTING C-di-GMP-binding domain + GMP derivative <br />
-	**[[5cfp]] – aSTING C-di-GMP-binding domain (mutant) + GMP derivative<br />
-	**[[5cfn]] – aSTING C-di-GMP-binding domain + AMP derivative <br />
-
-	}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 10:36, 10 April 2022

Michal Harel — Sun, 10 Apr 2022 10:36:39 GMT

←Older revision		Revision as of 10:36, 10 April 2022
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	== Structural highlights ==		== Structural highlights ==
	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A <scene name='57/573101/Cv/6'>Tyr residue from each monomer stacks</scene> against each of the purine moieties while an <scene name='57/573101/Cv/7'>Arg residue from each monomer forms hydrogen bonds to the dinucleotide</scene> <ref>PMID:23910378</ref>.		The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A <scene name='57/573101/Cv/6'>Tyr residue from each monomer stacks</scene> against each of the purine moieties while an <scene name='57/573101/Cv/7'>Arg residue from each monomer forms hydrogen bonds to the dinucleotide</scene> <ref>PMID:23910378</ref>.
		+	==3D structures of stimulator of interferon genes protein==

		+	[[Stimulator of interferon genes protein 3D structures]]
	</StructureSection>		</StructureSection>
	==3D structures of stimulator of interferon genes protein==		==3D structures of stimulator of interferon genes protein==

Alexander Berchansky at 12:56, 31 January 2021

Alexander Berchansky — Sun, 31 Jan 2021 12:56:38 GMT

←Older revision		Revision as of 12:56, 31 January 2021
Line 8:		Line 8:

	== Structural highlights ==		== Structural highlights ==
-	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A <scene name='57/573101/Cv/6'>Tyr residue from each monomer stacks</scene> against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.	+	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A <scene name='57/573101/Cv/6'>Tyr residue from each monomer stacks</scene> against each of the purine moieties while an <scene name='57/573101/Cv/7'>Arg residue from each monomer forms hydrogen bonds to the dinucleotide</scene> <ref>PMID:23910378</ref>.

	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:47, 31 January 2021

Alexander Berchansky — Sun, 31 Jan 2021 12:47:09 GMT

←Older revision		Revision as of 12:47, 31 January 2021
Line 8:		Line 8:

	== Structural highlights ==		== Structural highlights ==
-	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.	+	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A <scene name='57/573101/Cv/6'>Tyr residue from each monomer stacks</scene> against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.

	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:41, 31 January 2021

Alexander Berchansky — Sun, 31 Jan 2021 12:41:44 GMT

←Older revision		Revision as of 12:41, 31 January 2021
Line 8:		Line 8:

	== Structural highlights ==		== Structural highlights ==
-	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.	+	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.

	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:35, 31 January 2021

Alexander Berchansky — Sun, 31 Jan 2021 12:35:08 GMT

←Older revision		Revision as of 12:35, 31 January 2021
Line 8:		Line 8:

	== Structural highlights ==		== Structural highlights ==
-	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). ~~The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand.~~ A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.	+	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.

	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:34, 31 January 2021

Alexander Berchansky — Sun, 31 Jan 2021 12:34:29 GMT

←Older revision		Revision as of 12:34, 31 January 2021
Line 8:		Line 8:

	== Structural highlights ==		== Structural highlights ==
-	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene>. The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand. A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.	+	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand. A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.

	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:33, 31 January 2021

Alexander Berchansky — Sun, 31 Jan 2021 12:33:04 GMT

←Older revision		Revision as of 12:33, 31 January 2021
Line 8:		Line 8:

	== Structural highlights ==		== Structural highlights ==
-	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand. A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.	+	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene>. The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand. A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.

	</StructureSection>		</StructureSection>

Michal Harel at 11:22, 29 January 2021

Michal Harel — Fri, 29 Jan 2021 11:22:13 GMT

←Older revision		Revision as of 11:22, 29 January 2021
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	<StructureSection load='' size='350' side='right' caption='Structure of human STING CTD complex with c-GMP-AMP (PDB entry [[4loh]])' scene='57/573101/Cv/1'>		<StructureSection load='' size='350' side='right' caption='Structure of human STING CTD complex with c-GMP-AMP (PDB entry [[4loh]])' scene='57/573101/Cv/1'>
-		+
-	'''Stimulator of interferon genes''' (STING) ~~induces production of type I interferon when cells are infected by viruses, mycobacteria and intracellular parasites~~. STING ~~recognizes~~ and ~~binds~~ cyclic-~~di-GMP~~ produced by ~~bacteria and cyclic-~~GMP AMP ~~(cGAMP) produced~~ by ~~viruses~~. ~~The~~ C-terminal ~~domain (CTD) (residues 139-379~~ in ~~human) of STING binds cyclic-di-GMP~~. STING ~~is a facilitator of innate immune signaling~~<ref>PMID:~~26980676~~</ref>.	+	== Function ==
		+	'''Stimulator of interferon genes protein''' or '''transmembrane protein 173''' (STING) is an ER-associated membrane protein. STING signals immune responses in human and other animals. STING is activated by cyclic GMP-AMP produced by [[Cyclic GMP-AMP synthase]] whose activity is triggered by infections of DNA-containing pathogens<ref>PMID:30842659</ref>. A PLPLRT/SD conserved motif at the STING C-terminal plays a critical role in turning on the immune system to fight against viral infections<ref>PMID:31118511</ref>.
		+
		+	== Disease ==
		+	STING mutations are associated with autoimmune diseases<ref>PMID:26235147</ref>.

	== Structural highlights ==		== Structural highlights ==
-	The ~~<scene name='57/573101/Cv/4'>~~cyclic dinucleotide ~~binds~~ the STING ~~in a~~ U-shaped cleft between the 2 ~~monomers</scene>~~<ref>PMID:23910378</ref>. ~~Water molecules are shown as red spheres.~~	+	The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand. A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>.
		+
	</StructureSection>		</StructureSection>
		+	==3D structures of stimulator of interferon genes protein==

-	~~==3D structures of STING==~~	+	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	(Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}	+
	{{#tree:id=OrganizedByTopic\|openlevels=0\|		{{#tree:id=OrganizedByTopic\|openlevels=0\|
		+	*Stimulator of interferon genes protein; domains - C-di-GMP-binding 154-341; PLPLRT/SD motif 342-379

-	*Stimulator of interferon genes	+	**[[6nt5]] – hSTING - human - Cryo EM<br />
-		+	**[[4ef5]], [[4f5w]], [[4f9e]] – hSTING C-di-GMP-binding domain<br />
-	~~Domain: CTD 139-379~~	+	**[[4f5e]], [[6mx0]] – hSTING C-di-GMP-binding domain (mutant)<br />
-		+	**[[6iyf]] – pSTING C-di-GMP-binding domain - pig<br />
-	**[[6nt5]] – hSTING – human - Cryo EM <br />	+	**[[4kc0]] – mSTING C-di-GMP-binding domain - mouse<br />
-	**[[4ef5]], [[4f5w]], [[4f9e]] – hSTING ~~CTD~~<br />	+	**[[5gs5]] – rSTING C-di-GMP-binding domain - rat<br />
-	**[[4f5e]] – hSTING ~~CTD~~ (mutant) <br />	+	**[[6nt6]] – cSTING - chicken - Cryo EM<br />
-	**[[~~4jc5~~]], [[4kc0]] – mSTING ~~CTD~~ - mouse <br />	+	**[[5cfo]], [[5cfr]] – aSTING – anemone<br />
-	**[[6nt6]] – cSTING – chicken – Cryo EM <br />	+
-	**[[5cfo]], [[5cfr]] – ~~saSTING CTD~~ – ~~sea~~ anemone <br />	+

-	*Stimulator of interferon genes complex ~~with ligand~~	+	*Stimulator of interferon genes protein complex

-	**[[4ef4]], [[4f5y]], [[4f9g]], [[~~4emt~~]] – hSTING ~~CTD + c~~-di-GMP <br />	+	**[[4ef4]], [[4emt]], [[4emu]], [[4f5y]], [[4f9g]], [[6rm0]], [[6s86]] – hSTING C-di-GMP-binding domain + GMP derivative<br />
-	**[[4f5d]] – hSTING ~~CTD~~ (mutant) + ~~c-di-~~GMP <br />	+	**[[4f5d]] – hSTING C-di-GMP-binding domain (mutant) + GMP derivative <br />
-	**[[~~4ksy~~]] ~~– hSTING CTD + c-GAMP <br />~~	+	**[[6cff]], [[6cy7]] – hSTING C-di-GMP-binding domain + AMP derivative <br />
-	**[[~~5bqx~~]] – hSTING ~~CTD + c~~-GMP <br />	+	**[[4ksy]], [[4loh]], [[5bqx]], [[6dnk]], [[6xnp]], [[6s26]], [[6s27]] – hSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[4loh]], [[~~4loi~~]] – hSTING ~~CTD + c~~-di-GMP derivative<br />	+	**[[4loi]], [[6mx3]], [[6mxe]] – hSTING C-di-GMP-binding domain (mutant) + GMP-AMP derivative <br />
-	**[[~~6cff~~]] ~~– hSTING CTD + c-di-AMP <br />~~	+	**[[6dxg]], [[6dxl]], [[6ukm]], [[6uku]], [[6ukv]], [[6ukw]], [[6ukx]], [[6uky]], [[6ukz]], [[6ul0]] – hSTING C-di-GMP-binding domain + agonist <br />
-	**[[~~6dnk~~]] – hSTING ~~CTD + c~~-GMP-AMP <br />	+	**[[4qxo]] – hSTING C-di-GMP-binding domain + drug <br />
-	**[[~~4qxo~~]], [[~~4qxp~~]], [[~~4qxq~~]], [[~~4qxr~~]] ~~– hSTING CTD + chemptherapeutic agent DMXAA<br />~~	+	**[[4qxp]], [[4qxq]], [[4qxr]] – hSTING C-di-GMP-binding domain (mutant) + drug <br />
-	**[[~~6dxl~~]], [[~~6dxg~~]] – hSTING ~~CTD (mutant)~~ + ~~imidazole derivative~~ <br />	+	**[[5jej]] – hSTING PLPLRT/SD motif + IRF-3 CTD <br />
-	**[[~~6a06~~]] – ~~pSTING CTD + c~~-~~GAMP~~ - ~~pig~~<br />	+	**[[6o8b]], [[6o8c]] – hSTING PLPLRT/SD motif (mutant) + TBK1 <br />
-	**[[~~6a05~~]] – ~~pSTING CTD~~ + ~~purine derivative~~<br />	+	**[[6a03]], [[6a04]], [[6a05]], [[6a06]] – pSTING C-di-GMP-binding domain + ligand <br />
-	**[[~~6a04~~]] – ~~pSTING CTD~~ + c-~~di-GMP~~<br />	+	**[[4kby]] – mSTING C-di-GMP-binding domain+ GMP derivative<br />
-	**[[~~6a03~~]], [[~~6iyf~~]] – ~~pSTING CTD~~ + ~~c-di-AMP~~<br />	+	**[[4loj]], [[4lok]], [[4yp1]] – mSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[~~5jej~~]] – ~~hSTING residues 342~~-~~379 + IRF~~-3 <br />	+	**[[6xnn]] – mSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[4kby]] – mSTING ~~CTD + c~~-di-GMP <br />	+	**[[4lol]] – mSTING C-di-GMP-binding domain + drug <br />
-	**[[4loj]], [[4lok]] – mSTING ~~CTD + c~~-di-GMP derivative<br />	+	**[[4jc5]] – mSTING C-di-GMP-binding domain + immune activator <br />
-	**[[~~4yp1~~]] – mSTING ~~CTD + c~~-di-AMP derivative<br />	+	**[[5grm]] – rSTING C-di-GMP-binding domain + GMP-AMP derivative <br />
-	**[[4lol]] – mSTING ~~CTD~~ + ~~chemptherapeutic agent DMXAA~~<br />	+	**[[6nt7]], [[6nt8]] – cSTING + GMP-AMP derivative - Cryo EM<br />
-	**[[~~4kby~~]] – mSTING ~~CTD~~ + c-di-GMP <br />	+	**[[6nt9]] – cSTING + TBK1 - Cryo EM<br />
-	**[[6nt7]], [[6nt8]] – cSTING + GMP-AMP – Cryo EM <br />	+	**[[5cfl]], [[5cfm]], [[5cfq]] – aSTING C-di-GMP-binding domain + GMP derivative <br />
-	**[[6nt9]] – cSTING + TBK1 – Cryo EM <br />	+	**[[5cfp]] – aSTING C-di-GMP-binding domain (mutant) + GMP derivative<br />
-	**[[5cfl]] ~~– saSTING CTD + c-di-GMP <br />~~	+	**[[5cfn]] – aSTING C-di-GMP-binding domain + AMP derivative <br />
-	**[[~~5cfp~~]] ~~– saSTING CTD (mutant) + c-di-GMP <br />~~	+
-	**[[5cfq]] – ~~saSTING CTD + c~~-~~AMP~~-GMP <br />	+
-	**[[~~5cfm~~]] – ~~saSTING CTD + c~~-GMP <br />	+
-	**[[5cfn]] – ~~saSTING CTD + c~~-di-AMP <br />	+

	}}		}}

Michal Harel at 08:16, 12 November 2020

Michal Harel — Thu, 12 Nov 2020 08:16:33 GMT

←Older revision		Revision as of 08:16, 12 November 2020
Line 13:		Line 13:
	*Stimulator of interferon genes		*Stimulator of interferon genes

-	**[[4ef5]], [[4f5w]], [[4f9e]] – hSTING CTD ~~- human~~<br />	+	Domain: CTD 139-379
		+
		+	**[[6nt5]] – hSTING – human - Cryo EM <br />
		+	**[[4ef5]], [[4f5w]], [[4f9e]] – hSTING CTD<br />
	**[[4f5e]] – hSTING CTD (mutant) <br />		**[[4f5e]] – hSTING CTD (mutant) <br />
	**[[4jc5]], [[4kc0]] – mSTING CTD - mouse <br />		**[[4jc5]], [[4kc0]] – mSTING CTD - mouse <br />
Line 21:		Line 24:
	*Stimulator of interferon genes complex with ligand		*Stimulator of interferon genes complex with ligand

-	**[[4ef4]], [[4f5y]], [[4f9g]] ~~– hSTING CTD + c-di-GMP <br />~~	+	**[[4ef4]], [[4f5y]], [[4f9g]], [[4emt]] – hSTING CTD + c-di-GMP <br />
-	**[[4emt]] – hSTING ~~residues 155-341~~ + c-di-GMP <br />	+
	**[[4f5d]] – hSTING CTD (mutant) + c-di-GMP <br />		**[[4f5d]] – hSTING CTD (mutant) + c-di-GMP <br />
-	**[[4ksy]] – hSTING CTD + ~~cGAMP~~ <br />	+	**[[4ksy]] – hSTING CTD + c-GAMP <br />
	**[[5bqx]] – hSTING CTD + c-GMP <br />		**[[5bqx]] – hSTING CTD + c-GMP <br />
	**[[4loh]], [[4loi]] – hSTING CTD + c-di-GMP derivative<br />		**[[4loh]], [[4loi]] – hSTING CTD + c-di-GMP derivative<br />
		+	**[[6cff]] – hSTING CTD + c-di-AMP <br />
		+	**[[6dnk]] – hSTING CTD + c-GMP-AMP <br />
	**[[4qxo]], [[4qxp]], [[4qxq]], [[4qxr]] – hSTING CTD + chemptherapeutic agent DMXAA<br />		**[[4qxo]], [[4qxp]], [[4qxq]], [[4qxr]] – hSTING CTD + chemptherapeutic agent DMXAA<br />
-	**[[6a06]] – pSTING CTD + ~~cGAMP~~ - pig<br />	+	**[[6dxl]], [[6dxg]] – hSTING CTD (mutant) + imidazole derivative <br />
		+	**[[6a06]] – pSTING CTD + c-GAMP - pig<br />
	**[[6a05]] – pSTING CTD + purine derivative<br />		**[[6a05]] – pSTING CTD + purine derivative<br />
	**[[6a04]] – pSTING CTD + c-di-GMP<br />		**[[6a04]] – pSTING CTD + c-di-GMP<br />