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| <StructureSection load='4ous' size='340' side='right'caption='[[4ous]], [[Resolution|resolution]] 1.05Å' scene=''> | | <StructureSection load='4ous' size='340' side='right'caption='[[4ous]], [[Resolution|resolution]] 1.05Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4ous]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ous]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OUS FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oul|4oul]], [[4oum|4oum]]</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=4ous FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ous OCA], [https://pdbe.org/4ous PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ous RCSB], [https://www.ebi.ac.uk/pdbsum/4ous PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ous ProSAT]</span></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">caprin2, rng140, si:ch211-11c20.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>
| + | |
- | <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=4ous FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ous OCA], [http://pdbe.org/4ous PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ous RCSB], [http://www.ebi.ac.uk/pdbsum/4ous PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ous ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/CAPR2_DANRE CAPR2_DANRE]] May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons. Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation. May be involved in apoptosis (By similarity). | + | [https://www.uniprot.org/uniprot/CAPR2_DANRE CAPR2_DANRE] May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons. Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation. May be involved in apoptosis (By similarity). |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Li, L]] | + | [[Category: Li L]] |
- | [[Category: Song, X]] | + | [[Category: Song X]] |
- | [[Category: C1q domain]]
| + | |
- | [[Category: Signaling protein]]
| + | |
- | [[Category: Wnt signaling]]
| + | |
| Structural highlights
Function
CAPR2_DANRE May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons. Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation. May be involved in apoptosis (By similarity).
Publication Abstract from PubMed
Previously, we have identified Caprin-2 as a new regulator in canonical Wnt signaling through a mechanism of facilitating LRP5/6 phosphorylation; moreover, we found that its C-terminal C1q-related domain (Cap2_CRD) is required for this process. Here, we determined the crystal structures of Cap2_CRD from human and zebrafish, which both associate as a homotrimer with calcium located at the symmetric center. Surprisingly, the calcium binding-deficient mutant exists as a more stable trimer than its wild-type counterpart. Further studies showed that this Caprin-2 mutant disabled in binding calcium maintains the activity of promoting LRP5/6 phosphorylation, whereas the mutations disrupting Cap2_CRD homotrimer did impair such activity. Together, our findings suggested that the C-terminal CRD domain of Caprin-2 forms a flexible homotrimer mediated by calcium and that such trimeric assembly is required for Caprin-2 to regulate canonical Wnt signaling.
Structural insights into the C1q domain of Caprin-2 in canonical Wnt signaling.,Miao H, Jia Y, Xie S, Wang X, Zhao J, Chu Y, Zhou Z, Shi Z, Song X, Li L J Biol Chem. 2014 Dec 5;289(49):34104-13. doi: 10.1074/jbc.M114.591636. Epub 2014, Oct 20. PMID:25331957[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miao H, Jia Y, Xie S, Wang X, Zhao J, Chu Y, Zhou Z, Shi Z, Song X, Li L. Structural insights into the C1q domain of Caprin-2 in canonical Wnt signaling. J Biol Chem. 2014 Dec 5;289(49):34104-13. doi: 10.1074/jbc.M114.591636. Epub 2014, Oct 20. PMID:25331957 doi:http://dx.doi.org/10.1074/jbc.M114.591636
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