4gqt
From Proteopedia
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==N-terminal domain of C. elegans Hsp90== | ==N-terminal domain of C. elegans Hsp90== | ||
| - | <StructureSection load='4gqt' size='340' side='right' caption='[[4gqt]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='4gqt' size='340' side='right'caption='[[4gqt]], [[Resolution|resolution]] 2.15Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4gqt]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4gqt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GQT FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| - | <tr id=' | + | <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=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gqt OCA], [https://pdbe.org/4gqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gqt RCSB], [https://www.ebi.ac.uk/pdbsum/4gqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gqt ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/HSP90_CAEEL HSP90_CAEEL] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required to stabilize the daf-11/transmembrane guanylyl cyclases or another signal transduction component that regulates cGMP levels. Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation.<ref>PMID:10790386</ref> <ref>PMID:16466390</ref> |
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| + | ==See Also== | ||
| + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Chhor G]] |
| - | [[Category: | + | [[Category: Gu M]] |
| - | [[Category: | + | [[Category: Joachimiak A]] |
| - | [[Category: Morimoto | + | [[Category: Morimoto RI]] |
| - | + | [[Category: Osipiuk J]] | |
| - | [[Category: Osipiuk | + | [[Category: Van Oosten-Hawle P]] |
| - | [[Category: | + | |
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Current revision
N-terminal domain of C. elegans Hsp90
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