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8agl
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of human Heat shock protein 90-alpha N-terminal domain (Hsp90-NTD) variant K112R in complex with JMC31== | |
| - | + | <StructureSection load='8agl' size='340' side='right'caption='[[8agl]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8agl]] is a 2 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=8AGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AGL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0U:1-[2,4-bis(oxidanyl)-5-propan-2-yl-phenyl]-5-[4-[(cyclohexylmethylamino)methyl]phenyl]-~{N}-ethyl-1,2,3-triazole-4-carboxamide'>M0U</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8agl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8agl OCA], [https://pdbe.org/8agl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8agl RCSB], [https://www.ebi.ac.uk/pdbsum/8agl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8agl ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] 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.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref> |
| - | [[Category: Pozzi | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mangani S]] | ||
| + | [[Category: Maramai S]] | ||
| + | [[Category: Mazzorana M]] | ||
| + | [[Category: Pozzi C]] | ||
| + | [[Category: Tassone G]] | ||
Revision as of 16:41, 7 September 2022
Structure of human Heat shock protein 90-alpha N-terminal domain (Hsp90-NTD) variant K112R in complex with JMC31
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