7v69

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Current revision (14:08, 6 November 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7v69]] is a 5 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=7V69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V69 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7v69]] is a 5 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=7V69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V69 FirstGlance]. <br>
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</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=7v69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v69 OCA], [https://pdbe.org/7v69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v69 RCSB], [https://www.ebi.ac.uk/pdbsum/7v69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v69 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7v69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v69 OCA], [https://pdbe.org/7v69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v69 RCSB], [https://www.ebi.ac.uk/pdbsum/7v69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v69 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/GNAI1_HUMAN GNAI1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:17635935</ref> <ref>PMID:17264214</ref>
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[https://www.uniprot.org/uniprot/GBG2_HUMAN GBG2_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Muscarinic acetylcholine receptor|Muscarinic acetylcholine receptor]]
*[[Transducin 3D structures|Transducin 3D structures]]
*[[Transducin 3D structures|Transducin 3D structures]]
== References ==
== References ==

Current revision

Cryo-EM structure of a class A GPCR-G protein complex

PDB ID 7v69

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