8vk3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of mouse RyR1 in complex with S100A1 (EGTA-only dataset)== | |
| - | + | <StructureSection load='8vk3' size='340' side='right'caption='[[8vk3]], [[Resolution|resolution]] 3.21Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8vk3]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VK3 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.21Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | [[Category: Marks | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8vk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vk3 OCA], [https://pdbe.org/8vk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vk3 RCSB], [https://www.ebi.ac.uk/pdbsum/8vk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vk3 ProSAT]</span></td></tr> |
| - | [[Category: Weninger | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FKB1A_MOUSE FKB1A_MOUSE] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Marks AR]] | ||
| + | [[Category: Weninger G]] | ||
Revision as of 11:31, 24 January 2024
Structure of mouse RyR1 in complex with S100A1 (EGTA-only dataset)
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