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| | ==Solution structure of rat RIP2 caspase recruitment domain== | | ==Solution structure of rat RIP2 caspase recruitment domain== |
| - | <StructureSection load='6gwm' size='340' side='right'caption='[[6gwm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6gwm' size='340' side='right'caption='[[6gwm]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gwm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GWM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gwm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GWM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ripk2, rCG_54865 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | </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=6gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwm OCA], [https://pdbe.org/6gwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gwm RCSB], [https://www.ebi.ac.uk/pdbsum/6gwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gwm ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=6gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwm OCA], [http://pdbe.org/6gwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gwm RCSB], [http://www.ebi.ac.uk/pdbsum/6gwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gwm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G3V783_RAT G3V783_RAT]] Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains.[PIRNR:PIRNR037921] | + | [https://www.uniprot.org/uniprot/G3V783_RAT G3V783_RAT] Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains.[PIRNR:PIRNR037921] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6gwm" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6gwm" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]] | |
| - | [[Category: Arseniev, A S]] | |
| - | [[Category: Artemieva, L E]] | |
| - | [[Category: Goncharuk, S A]] | |
| - | [[Category: Mineev, K S]] | |
| - | [[Category: Card]] | |
| - | [[Category: Caspase recruitment domain]] | |
| | [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
| - | [[Category: Rip2]] | + | [[Category: Arseniev AS]] |
| - | [[Category: Signaling protein]] | + | [[Category: Artemieva LE]] |
| | + | [[Category: Goncharuk SA]] |
| | + | [[Category: Mineev KS]] |
| Structural highlights
Function
G3V783_RAT Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains.[PIRNR:PIRNR037921]
Publication Abstract from PubMed
RIP2, one of the RIP kinases, interacts with p75 neurotrophin receptor, regulating the neuron survival, and with NOD1 and NOD2 proteins, causing the innate immune response against gram-negative and gram-positive bacteria via its caspase recruitment domain (CARD). This makes RIP2 a prospective target for novel therapies, aimed to modulate the inflammatory diseases and neurogenesis/neurodegeneration. Several studies report the problems with the stability of human RIP2 CARD and its production in bacterial hosts, which is a prerequisite for the structural investigation with solution NMR spectroscopy. In the present work, we report the high yield production and refolding protocols and resolve the structure of rat RIP2 CARD. The structure reveals the important differences to the previously published conformation of the homologous human protein. Using solution NMR, we characterized the intramolecular mobility and pH-dependent behavior of RIP2 CARD, and found the propensity of the protein to form high-order oligomers at physiological pH while being monomeric under acidic conditions. The oligomerization of protein may be explained, based on the electrostatic properties of its surface. Analysis of the structure and sequences of homologous proteins reveals the residues which are significant for the unusual fold of RIP2 CARD domains from different species. The high-throughput protein production/refolding protocols and proposed explanation for the protein oligomerization, provide an opportunity to design the stabilized variants of RIP2 CARD, which could be used to study the structural details of RIP2/NOD1/NOD2 interaction and perform the rational drug design.
CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions.,Goncharuk SA, Artemieva LE, Tabakmakher VM, Arseniev AS, Mineev KS PLoS One. 2018 Oct 23;13(10):e0206244. doi: 10.1371/journal.pone.0206244., eCollection 2018. PMID:30352081[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Goncharuk SA, Artemieva LE, Tabakmakher VM, Arseniev AS, Mineev KS. CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions. PLoS One. 2018 Oct 23;13(10):e0206244. doi: 10.1371/journal.pone.0206244., eCollection 2018. PMID:30352081 doi:http://dx.doi.org/10.1371/journal.pone.0206244
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