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| | <StructureSection load='3rg0' size='340' side='right'caption='[[3rg0]], [[Resolution|resolution]] 2.57Å' scene=''> | | <StructureSection load='3rg0' size='340' side='right'caption='[[3rg0]], [[Resolution|resolution]] 2.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rg0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RG0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rg0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RG0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.57Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Calr ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3rg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rg0 OCA], [https://pdbe.org/3rg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rg0 RCSB], [https://www.ebi.ac.uk/pdbsum/3rg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rg0 ProSAT]</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=3rg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rg0 OCA], [https://pdbe.org/3rg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rg0 RCSB], [https://www.ebi.ac.uk/pdbsum/3rg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rg0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CALR_MOUSE CALR_MOUSE]] 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:20880849</ref> <ref>PMID:21652723</ref>
| + | [https://www.uniprot.org/uniprot/CALR_MOUSE CALR_MOUSE] 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:20880849</ref> <ref>PMID:21652723</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Brockmeier, U]] | + | [[Category: Brockmeier U]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gehring K]] |
| - | [[Category: Kozlov, G]] | + | [[Category: Kozlov G]] |
| - | [[Category: Pocanschi, C L]] | + | [[Category: Pocanschi CL]] |
| - | [[Category: Williams, D B]] | + | [[Category: Williams DB]] |
| - | [[Category: Beta-sandwich]]
| + | |
| - | [[Category: Calcium binding]]
| + | |
| - | [[Category: Carbohydrate binding]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Monoglucosylated proteins binding]]
| + | |
| Structural highlights
Function
CALR_MOUSE 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).[1] [2]
Publication Abstract from PubMed
Calreticulin and calnexin are key components in maintaining the quality control of glycoprotein folding within the endoplasmic reticulum. While their lectin function of binding monoglucosylated sugar moieties of glycoproteins is well documented, their chaperone activity in suppressing protein aggregation is less well understood. Here, we use a series of deletion mutants of calreticulin to demonstrate that its aggregation suppression function resides primarily within its lectin domain. Using hydrophobic peptides as substrate mimetics, we show that aggregation suppression is mediated through a single polypeptide binding site that exhibits a Kd for peptides of 0.5-1 muM. This site is distinct from the oligosaccharide binding site and differs from previously identified sites of binding to thrombospondin and GABARAP. Although the arm domain of calreticulin was incapable of suppressing aggregation or binding hydrophobic peptides on its own, it did contribute to aggregation suppression in the context of the whole molecule. The high resolution X-ray crystal structure of calreticulin with a partially truncated arm domain reveals a marked difference in the relative orientations of the arm and lectin domains when compared to calnexin. Furthermore, a hydrophobic patch was detected on the arm domain that mediates crystal packing and may contribute to calreticulin's chaperone function.
Structural and functional relationships between the lectin and arm domains of calreticulin.,Pocanschi CL, Kozlov G, Brockmeier U, Brockmeier A, Williams DB, Gehring K J Biol Chem. 2011 Jun 7. PMID:21652723[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kozlov G, Pocanschi CL, Rosenauer A, Bastos-Aristizabal S, Gorelik A, Williams DB, Gehring K. Structural basis of carbohydrate recognition by calreticulin. J Biol Chem. 2010 Dec 3;285(49):38612-20. Epub 2010 Sep 29. PMID:20880849 doi:10.1074/jbc.M110.168294
- ↑ Pocanschi CL, Kozlov G, Brockmeier U, Brockmeier A, Williams DB, Gehring K. Structural and functional relationships between the lectin and arm domains of calreticulin. J Biol Chem. 2011 Jun 7. PMID:21652723 doi:10.1074/jbc.M111.258467
- ↑ Pocanschi CL, Kozlov G, Brockmeier U, Brockmeier A, Williams DB, Gehring K. Structural and functional relationships between the lectin and arm domains of calreticulin. J Biol Chem. 2011 Jun 7. PMID:21652723 doi:10.1074/jbc.M111.258467
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