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| ==Crystal structure of CARMA1 CARD== | | ==Crystal structure of CARMA1 CARD== |
| <StructureSection load='4i16' size='340' side='right' caption='[[4i16]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='4i16' size='340' side='right'caption='[[4i16]], [[Resolution|resolution]] 1.75Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4i16]] is a 1 chain structure with sequence from [http://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=4I16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I16 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4i16]] 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=4I16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I16 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.751Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Card11 ([http://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=SO4:SULFATE+ION'>SO4</scene></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=4i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i16 OCA], [http://pdbe.org/4i16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i16 RCSB], [http://www.ebi.ac.uk/pdbsum/4i16 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i16 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=4i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i16 OCA], [https://pdbe.org/4i16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i16 RCSB], [https://www.ebi.ac.uk/pdbsum/4i16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i16 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CAR11_MOUSE CAR11_MOUSE]] Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Activates NF-kappa-B via BCL10 and IKK. Stimulates the phosphorylation of BCL10 (By similarity). | | [https://www.uniprot.org/uniprot/CAR11_MOUSE CAR11_MOUSE] Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Activates NF-kappa-B via BCL10 and IKK. Stimulates the phosphorylation of BCL10 (By similarity). |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The CBM complex (CARMA1, BCL10 and MALT1) plays a crucial role in B and T lymphocyte activation. CARMA1 serves as a scaffold for BCL10, MALT1 and other effector proteins and regulates various signaling pathways related to the immune response. The assembly of CARMA1 and BCL10 is mediated through a CARD-CARD interaction. Here, we report the crystal structure of the CARD domain of CARMA1 at a resolution of 1.75 A. The structure consists of six helices, as previously determined for CARD domains. Structural and computational analysis identified the binding interface between CARMA1-CARD and BCL10-CARD, which consists of a basic patch in CARMA1 and an acidic patch in BCL10. Site-directed mutagenesis, co-immunoprecipitation and an NF-kappaB activation assay confirmed that the interface is necessary for association and downstream signaling. Our studies provide molecular insight into the assembly of CARMA1 and BCL10.
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| Structural insights into the assembly of CARMA1 and BCL10.,Li S, Yang X, Shao J, Shen Y PLoS One. 2012;7(8):e42775. doi: 10.1371/journal.pone.0042775. Epub 2012 Aug 3. PMID:22880103<ref>PMID:22880103</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4i16" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Lk3 transgenic mice]] | | [[Category: Large Structures]] |
| [[Category: Li, S]] | | [[Category: Mus musculus]] |
| [[Category: Shen, Y]] | | [[Category: Li S]] |
| [[Category: Yang, X]] | | [[Category: Shen Y]] |
| [[Category: Bcl10 and malt1 binding]] | | [[Category: Yang X]] |
| [[Category: Cbm complex]]
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| [[Category: Helix bundle]]
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| [[Category: Phosphorylation]]
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| [[Category: Scaffold protein]]
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| [[Category: Signaling protein]]
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