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3o2f

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{{STRUCTURE_3o2f| PDB=3o2f | SCENE= }}
 
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===Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54===
 
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{{ABSTRACT_PUBMED_23995768}}
 
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==Function==
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==Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54==
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[[http://www.uniprot.org/uniprot/ENPL_CANFA ENPL_CANFA]] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
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<StructureSection load='3o2f' size='340' side='right'caption='[[3o2f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[3o2f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O2F FirstGlance]. <br>
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[[3o2f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O2F OCA].
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=P54:8-[(2,4-DIMETHYLPHENYL)SULFANYL]-3-PENT-4-YN-1-YL-3H-PURIN-6-AMINE'>P54</scene></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=3o2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o2f OCA], [https://pdbe.org/3o2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o2f RCSB], [https://www.ebi.ac.uk/pdbsum/3o2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o2f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
==See Also==
==See Also==
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*[[Endoplasmin|Endoplasmin]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:023995768</ref><references group="xtra"/><references/>
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[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
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[[Category: Gewirth, D T.]]
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[[Category: Large Structures]]
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[[Category: Seidler, P M.]]
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[[Category: Gewirth DT]]
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[[Category: Chaperone-inhibitor complex]]
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[[Category: Seidler PM]]
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[[Category: Hsp90 heat-shock protein]]
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Current revision

Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54

PDB ID 3o2f

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