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| | <StructureSection load='3v4l' size='340' side='right'caption='[[3v4l]], [[Resolution|resolution]] 3.15Å' scene=''> | | <StructureSection load='3v4l' size='340' side='right'caption='[[3v4l]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3v4l]] is a 2 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=3V4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V4L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3v4l]] is a 2 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=3V4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V4L FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CF0:FLUOROMETHANE'>CF0</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</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]] 3.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v4o|3v4o]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CF0:FLUOROMETHANE'>CF0</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Malt1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3v4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4l OCA], [https://pdbe.org/3v4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v4l RCSB], [https://www.ebi.ac.uk/pdbsum/3v4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4l 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=3v4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4l OCA], [https://pdbe.org/3v4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v4l RCSB], [https://www.ebi.ac.uk/pdbsum/3v4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MALT1_MOUSE MALT1_MOUSE]] Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity (By similarity). MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (By similarity).[UniProtKB:Q9UDY8]
| + | [https://www.uniprot.org/uniprot/MALT1_MOUSE MALT1_MOUSE] Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity (By similarity). MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (By similarity).[UniProtKB:Q9UDY8] |
| | <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: Renatus, M]] | + | [[Category: Renatus M]] |
| - | [[Category: Wiesmann, C]] | + | [[Category: Wiesmann C]] |
| - | [[Category: Caspase]]
| + | |
| - | [[Category: Cytosol]]
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| - | [[Category: Hydrolase-inhibitor complex]]
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| - | [[Category: Hydrolyse]]
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| - | [[Category: Ig like]]
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| - | [[Category: Traf6]]
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| Structural highlights
Function
MALT1_MOUSE Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity (By similarity). MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (By similarity).[UniProtKB:Q9UDY8]
Publication Abstract from PubMed
The formation of the CBM (CARD11-BCL10-MALT1) complex is pivotal for antigen-receptor-mediated activation of the transcription factor NF-kappaB. Signaling is dependent on MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1), which not only acts as a scaffolding protein but also possesses proteolytic activity mediated by its caspase-like domain. It remained unclear how the CBM activates MALT1. Here, we provide biochemical and structural evidence that MALT1 activation is dependent on its dimerization and show that mutations at the dimer interface abrogate activity in cells. The unliganded protease presents itself in a dimeric yet inactive state and undergoes substantial conformational changes upon substrate binding. These structural changes also affect the conformation of the C-terminal Ig-like domain, a domain that is required for MALT1 activity. Binding to the active site is coupled to a relative movement of caspase and Ig-like domains. MALT1 binding partners thus may have the potential of tuning MALT1 protease activity without binding directly to the caspase domain.
Structural Determinants of MALT1 Protease Activity.,Wiesmann C, Leder L, Blank J, Bernardi A, Melkko S, Decock A, D'Arcy A, Villard F, Erbel P, Hughes N, Freuler F, Nikolay R, Alves J, Bornancin F, Renatus M J Mol Biol. 2012 Feb 23. PMID:22366302[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wiesmann C, Leder L, Blank J, Bernardi A, Melkko S, Decock A, D'Arcy A, Villard F, Erbel P, Hughes N, Freuler F, Nikolay R, Alves J, Bornancin F, Renatus M. Structural Determinants of MALT1 Protease Activity. J Mol Biol. 2012 Feb 23. PMID:22366302 doi:10.1016/j.jmb.2012.02.018
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