1qy8

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{{Seed}}
 
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[[Image:1qy8.png|left|200px]]
 
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==Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol==
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The line below this paragraph, containing "STRUCTURE_1qy8", creates the "Structure Box" on the page.
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<StructureSection load='1qy8' size='340' side='right'caption='[[1qy8]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qy8]] is a 1 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=1QY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QY8 FirstGlance]. <br>
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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]] 1.85&#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=RDI:RADICICOL'>RDI</scene></td></tr>
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{{STRUCTURE_1qy8| PDB=1qy8 | SCENE= }}
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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=1qy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qy8 OCA], [https://pdbe.org/1qy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qy8 RCSB], [https://www.ebi.ac.uk/pdbsum/1qy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qy8 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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/1qy8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qy8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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GRP94, the endoplasmic reticulum (ER) paralog of the chaperone Hsp90, plays an essential role in the structural maturation or secretion of a subset of proteins destined for transport to the cell surface, such as the Toll-like receptors 2 and 4, and IgG, respectively. GRP94 differs from cytoplasmic Hsp90 by exhibiting very weak ATP binding and hydrolysis activity. GRP94 also binds selectively to a series of substituted adenosine analogs. The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members. The structures also identify a putative subdomain that may act as a ligand-responsive switch. The residues of the charged region fold into a disordered loop whose termini are ordered and continue the twisted beta sheet that forms the structural core of the N-domain. This continuation of the beta sheet past the charged domain suggests a structural basis for the association of the N-terminal and middle domains of the full-length chaperone.
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===Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol===
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Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.,Soldano KL, Jivan A, Nicchitta CV, Gewirth DT J Biol Chem. 2003 Nov 28;278(48):48330-8. Epub 2003 Sep 11. PMID:12970348<ref>PMID:12970348</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1qy8" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12970348}}, adds the Publication Abstract to the page
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12970348 is the PubMed ID number.
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_12970348}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1QY8 is a 1 chain structure of 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=1QY8 OCA].
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==Reference==
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<ref group="xtra">PMID:12970348</ref><references group="xtra"/>
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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: Jivan, A.]]
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[[Category: Gewirth DT]]
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[[Category: Nicchitta, C V.]]
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[[Category: Jivan A]]
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[[Category: Soldano, K L.]]
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[[Category: Nicchitta CV]]
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[[Category: Gp96]]
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[[Category: Soldano KL]]
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[[Category: Grp94]]
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[[Category: Hsp90]]
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[[Category: Radicicol]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:05:15 2009''
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Current revision

Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol

PDB ID 1qy8

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