8qeh: Difference between revisions

Latest revision as of 06:21, 19 March 2025

Crystal structure of the G11 protein heterotrimer bound to FR900359 inhibitor

Structural highlights

8qeh is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.43Å
Ligands:	ALA, CL, DAM, DMS, EDO, GDP, HF2, HL2, MAA, OTH, PPI, UDL, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

GNA11_HUMAN Phakomatosis cesioflammea;Uveal melanoma;Phakomatosis cesiomarmorata;Autosomal dominant hypocalcemia;Familial hypocalciuric hypercalcemia type 2;Cutis marmorata telangiectatica congenita. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.

Function

GNA11_HUMAN Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:31073061). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:31073061). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:31073061). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:31073061). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:31073061). Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation: activates phospholipase C-beta: following GPCR activation, GNA11 activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:31073061). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (PubMed:27852822). Together with GNAQ, required for heart development (By similarity).[UniProtKB:P21278]^[1] ^[2]

References

↑ Alvarez-Curto E, Inoue A, Jenkins L, Raihan SZ, Prihandoko R, Tobin AB, Milligan G. Targeted Elimination of G Proteins and Arrestins Defines Their Specific Contributions to Both Intensity and Duration of G Protein-coupled Receptor Signaling. J Biol Chem. 2016 Dec 30;291(53):27147-27159. PMID:27852822 doi:10.1074/jbc.M116.754887
↑ Maeda S, Qu Q, Robertson MJ, Skiniotis G, Kobilka BK. Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes. Science. 2019 May 10;364(6440):552-557. doi: 10.1126/science.aaw5188. PMID:31073061 doi:https://dx.doi.org/10.1126/science.aaw5188

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OCA

[1] Alvarez-Curto E, Inoue A, Jenkins L, Raihan SZ, Prihandoko R, Tobin AB, Milligan G. Targeted Elimination of G Proteins and Arrestins Defines Their Specific Contributions to Both Intensity and Duration of G Protein-coupled Receptor Signaling. J Biol Chem. 2016 Dec 30;291(53):27147-27159. PMID:27852822 doi:10.1074/jbc.M116.754887

[2] Maeda S, Qu Q, Robertson MJ, Skiniotis G, Kobilka BK. Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes. Science. 2019 May 10;364(6440):552-557. doi: 10.1126/science.aaw5188. PMID:31073061 doi:https://dx.doi.org/10.1126/science.aaw5188

[1]

[2]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8qeh is ON HOLD
+==Crystal structure of the G11 protein heterotrimer bound to FR900359 inhibitor==
+<StructureSection load='8qeh' size='340' side='right'caption='[[8qeh]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8qeh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QEH FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.43&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAM:N-METHYL-ALPHA-BETA-DEHYDROALANINE'>DAM</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=HF2:(2R)-2-HYDROXY-3-PHENYLPROPANOIC+ACID'>HF2</scene>, <scene name='pdbligand=HL2:(2S,3R)-2-AMINO-3-HYDROXY-4-METHYLPENTANOIC+ACID'>HL2</scene>, <scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=OTH:N,O-DIMETHYL-L-THREONINE'>OTH</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene>, <scene name='pdbligand=UDL:(2~{S},3~{R})-2-acetamido-4-methyl-3-oxidanyl-pentanoic+acid'>UDL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8qeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qeh OCA], [https://pdbe.org/8qeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qeh RCSB], [https://www.ebi.ac.uk/pdbsum/8qeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qeh ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/GNA11_HUMAN GNA11_HUMAN] Phakomatosis cesioflammea;Uveal melanoma;Phakomatosis cesiomarmorata;Autosomal dominant hypocalcemia;Familial hypocalciuric hypercalcemia type 2;Cutis marmorata telangiectatica congenita. The disease is caused by variants affecting the gene represented in this entry.  The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/GNA11_HUMAN GNA11_HUMAN] Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:31073061). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:31073061). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:31073061). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:31073061). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:31073061). Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation: activates phospholipase C-beta: following GPCR activation, GNA11 activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:31073061). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (PubMed:27852822). Together with GNAQ, required for heart development (By similarity).[UniProtKB:P21278]<ref>PMID:27852822</ref> <ref>PMID:31073061</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Deupi X]]
+[[Category: Guixa-Gonzalez R]]
+[[Category: Muehle J]]
+[[Category: Rodrigues MJ]]
+[[Category: Schertler GFX]]

8qeh: Difference between revisions

Latest revision as of 06:21, 19 March 2025

Crystal structure of the G11 protein heterotrimer bound to FR900359 inhibitor

Structural highlights

Disease

Function

References

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