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5v90

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Current revision (13:44, 4 October 2023) (edit) (undo)
 
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<StructureSection load='5v90' size='340' side='right'caption='[[5v90]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
<StructureSection load='5v90' size='340' side='right'caption='[[5v90]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5v90]] is a 4 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=5V90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V90 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5v90]] is a 4 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=5V90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V90 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=GOL:GLYCEROL'>GOL</scene></td></tr>
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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]] 3.255&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v8z|5v8z]]</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></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERP29, C12orf8, ERP28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CALR, CRTC ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5v90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v90 OCA], [https://pdbe.org/5v90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v90 RCSB], [https://www.ebi.ac.uk/pdbsum/5v90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v90 ProSAT]</span></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=5v90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v90 OCA], [http://pdbe.org/5v90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v90 RCSB], [http://www.ebi.ac.uk/pdbsum/5v90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v90 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ERP29_HUMAN ERP29_HUMAN]] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. [[http://www.uniprot.org/uniprot/CALR_HUMAN CALR_HUMAN]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:7876246</ref> <ref>PMID:11149926</ref>
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[https://www.uniprot.org/uniprot/ERP29_HUMAN ERP29_HUMAN] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
<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==
*[[Calreticulin 3D structures|Calreticulin 3D structures]]
*[[Calreticulin 3D structures|Calreticulin 3D structures]]
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*[[ER-resident protein|ER-resident protein]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gehring, K]]
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[[Category: Gehring K]]
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[[Category: Kozlov, G]]
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[[Category: Kozlov G]]
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[[Category: Munoz-Escobar, J]]
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[[Category: Munoz-Escobar J]]
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[[Category: Chaperone]]
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[[Category: Protein binding]]
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[[Category: Protein folding]]
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Current revision

Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin

PDB ID 5v90

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