8shq
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==CCT G beta 5 complex closed state 12== | |
| - | + | <StructureSection load='8shq' size='340' side='right'caption='[[8shq]], [[Resolution|resolution]] 2.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8shq]] is a 18 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=8SHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SHQ 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]] 2.9Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | [[Category: Sass | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8shq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8shq OCA], [https://pdbe.org/8shq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8shq RCSB], [https://www.ebi.ac.uk/pdbsum/8shq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8shq ProSAT]</span></td></tr> |
| - | [[Category: Shen | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/PHLP_HUMAN PHLP_HUMAN] Acts as a positive regulator of hedgehog signaling and regulates ciliary function.[UniProtKB:Q9DBX2] Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers. Acts as a negative regulator of heterotrimeric G proteins assembly by trapping the preloaded G beta subunits inside the CCT chaperonin. |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sass M]] | ||
| + | [[Category: Shen PS]] | ||
| + | [[Category: Wang S]] | ||
| + | [[Category: Willardson BM]] | ||
Current revision
CCT G beta 5 complex closed state 12
| |||||||||||
