2op6: Difference between revisions
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<StructureSection load='2op6' size='340' side='right'caption='[[2op6]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2op6' size='340' side='right'caption='[[2op6]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2op6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2op6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OP6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2op6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2op6 OCA], [https://pdbe.org/2op6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2op6 RCSB], [https://www.ebi.ac.uk/pdbsum/2op6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2op6 ProSAT], [https://www.topsan.org/Proteins/MCSG/2op6 TOPSAN]</span></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=2op6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2op6 OCA], [https://pdbe.org/2op6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2op6 RCSB], [https://www.ebi.ac.uk/pdbsum/2op6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2op6 ProSAT], [https://www.topsan.org/Proteins/MCSG/2op6 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BIBH_CAEEL BIBH_CAEEL] Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions (PubMed:15716356). Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion (PubMed:15716356).[UniProtKB:P11021]<ref>PMID:15716356</ref> | |||
== 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]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caenorhabditis elegans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Duggan | [[Category: Duggan E]] | ||
[[Category: Gu | [[Category: Gu M]] | ||
[[Category: Joachimiak | [[Category: Joachimiak A]] | ||
[[Category: Morimoto RI]] | |||
[[Category: Morimoto | [[Category: Osipiuk J]] | ||
[[Category: Osipiuk | [[Category: Voisine C]] | ||
[[Category: Voisine | |||
Latest revision as of 13:46, 30 August 2023
Peptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegansPeptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegans
Structural highlights
FunctionBIBH_CAEEL Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions (PubMed:15716356). Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion (PubMed:15716356).[UniProtKB:P11021][1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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