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| | <StructureSection load='1qy8' size='340' side='right'caption='[[1qy8]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='1qy8' size='340' side='right'caption='[[1qy8]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qy8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canlf Canlf]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1QY8 FirstGlance]. <br> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qy5|1qy5]]</div></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 CANLF])</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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qy8 OCA], [http://pdbe.org/1qy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qy8 RCSB], [http://www.ebi.ac.uk/pdbsum/1qy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qy8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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). | + | [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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| - | *[[Proteinase|Proteinase]] | |
| | *[[Proteinase 3D structures|Proteinase 3D structures]] | | *[[Proteinase 3D structures|Proteinase 3D structures]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Canlf]] | + | [[Category: Canis lupus familiaris]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gewirth, D T]] | + | [[Category: Gewirth DT]] |
| - | [[Category: Jivan, A]] | + | [[Category: Jivan A]] |
| - | [[Category: Nicchitta, C V]] | + | [[Category: Nicchitta CV]] |
| - | [[Category: Soldano, K L]] | + | [[Category: Soldano KL]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Gp96]]
| + | |
| - | [[Category: Grp94]]
| + | |
| - | [[Category: Hsp90]]
| + | |
| - | [[Category: Radicicol]]
| + | |
| Structural highlights
Function
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).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Soldano KL, Jivan A, Nicchitta CV, Gewirth DT. Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation. J Biol Chem. 2003 Nov 28;278(48):48330-8. Epub 2003 Sep 11. PMID:12970348 doi:http://dx.doi.org/10.1074/jbc.M308661200
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