4nh8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity== | |
| + | <StructureSection load='4nh8' size='340' side='right'caption='[[4nh8]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4nh8]] is a 1 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=4NH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NH8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2LC:2-FLUORO-6-[(3S)-TETRAHYDROFURAN-3-YLAMINO]-4-(3,6,6-TRIMETHYL-4-OXO-4,5,6,7-TETRAHYDRO-1H-INDOL-1-YL)BENZAMIDE'>2LC</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=4nh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nh8 OCA], [https://pdbe.org/4nh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nh8 RCSB], [https://www.ebi.ac.uk/pdbsum/4nh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nh8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| - | + | ==See Also== | |
| - | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ernst JT]] | ||
| + | [[Category: Zuccola HJ]] | ||
Current revision
Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity
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