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4nh8

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==Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity==
==Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity==
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<StructureSection load='4nh8' size='340' side='right' caption='[[4nh8]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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<StructureSection load='4nh8' size='340' side='right'caption='[[4nh8]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nh8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NH8 FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nh7|4nh7]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nh8 OCA], [http://pdbe.org/4nh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nh8 RCSB], [http://www.ebi.ac.uk/pdbsum/4nh8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nh8 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4nh8" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4nh8" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Ernst, J T]]
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[[Category: Large Structures]]
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[[Category: Zuccola, H J]]
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[[Category: Ernst JT]]
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[[Category: A/b protein]]
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[[Category: Zuccola HJ]]
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[[Category: Chaperone]]
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Revision as of 08:28, 11 January 2023

Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity

PDB ID 4nh8

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