8el8
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8el8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EL8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8el8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EL8 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=8el8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8el8 OCA], [https://pdbe.org/8el8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8el8 RCSB], [https://www.ebi.ac.uk/pdbsum/8el8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8el8 ProSAT]</span></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=8el8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8el8 OCA], [https://pdbe.org/8el8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8el8 RCSB], [https://www.ebi.ac.uk/pdbsum/8el8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8el8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GNAL_HUMAN GNAL_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters. | [https://www.uniprot.org/uniprot/GNAL_HUMAN GNAL_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mammalian Ric-8 proteins act as chaperones to regulate the cellular abundance of heterotrimeric G protein alpha subunits. The Ric-8A isoform chaperones Galphai/o, Galpha12/13, and Galphaq/11 subunits, while Ric-8B acts on Galphas/olf subunits. Here, we determined cryoelectron microscopy (cryo-EM) structures of Ric-8B in complex with Galphas and Galphaolf, revealing isoform differences in the relative positioning and contacts between the C-terminal alpha5 helix of Galpha within the concave pocket formed by Ric-8 alpha-helical repeat elements. Despite the overall architectural similarity with our earlier structures of Ric-8A complexed to Galphaq and Galphai1, Ric-8B distinctly accommodates an extended loop found only in Galphas/olf proteins. The structures, along with results from Ric-8 protein thermal stability assays and cell-based Galphaolf folding assays, support a requirement for the Galpha C-terminal region for binding specificity, and highlight that multiple structural elements impart specificity for Ric-8/G protein binding. | ||
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| + | Structures of Ric-8B in complex with Galpha protein folding clients reveal isoform specificity mechanisms.,Papasergi-Scott MM, Kwarcinski FE, Yu M, Panova O, Ovrutsky AM, Skiniotis G, Tall GG Structure. 2023 May 4;31(5):553-564.e7. doi: 10.1016/j.str.2023.02.011. Epub 2023 , Mar 16. PMID:36931277<ref>PMID:36931277</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8el8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
CryoEM structure of Resistance to Inhibitors of Cholinesterase-8B (Ric-8B) in complex with olfactory G protein alpha olf
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