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3qdd

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==HSP90A N-terminal domain in complex with BIIB021==
==HSP90A N-terminal domain in complex with BIIB021==
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<StructureSection load='3qdd' size='340' side='right' caption='[[3qdd]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
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<StructureSection load='3qdd' size='340' side='right'caption='[[3qdd]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qdd]] 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=3QDD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QDD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qdd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDD 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=94M:6-CHLORO-9-[(4-METHOXY-3,5-DIMETHYLPYRIDIN-2-YL)METHYL]-9H-PURIN-2-AMINE'>94M</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=94M:6-CHLORO-9-[(4-METHOXY-3,5-DIMETHYLPYRIDIN-2-YL)METHYL]-9H-PURIN-2-AMINE'>94M</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([https://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=3qdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdd OCA], [http://pdbe.org/3qdd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qdd RCSB], [http://www.ebi.ac.uk/pdbsum/3qdd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdd ProSAT]</span></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=3qdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdd OCA], [https://pdbe.org/3qdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qdd RCSB], [https://www.ebi.ac.uk/pdbsum/3qdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdd ProSAT]</span></td></tr>
</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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==See Also==
==See Also==
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*[[Heat Shock Proteins|Heat Shock Proteins]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Arndt, J W]]
[[Category: Arndt, J W]]
[[Category: Biamonte, M A]]
[[Category: Biamonte, M A]]
[[Category: Atpase]]
[[Category: Atpase]]
[[Category: Chaperone-chaperone inhibitor complex]]
[[Category: Chaperone-chaperone inhibitor complex]]

Revision as of 06:03, 8 June 2022

HSP90A N-terminal domain in complex with BIIB021

PDB ID 3qdd

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