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| | <StructureSection load='2nz7' size='340' side='right'caption='[[2nz7]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2nz7' size='340' side='right'caption='[[2nz7]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nz7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NZ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nz7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NZ7 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CARD4, NOD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2nz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nz7 OCA], [https://pdbe.org/2nz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nz7 RCSB], [https://www.ebi.ac.uk/pdbsum/2nz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nz7 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=2nz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nz7 OCA], [https://pdbe.org/2nz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nz7 RCSB], [https://www.ebi.ac.uk/pdbsum/2nz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nz7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NOD1_HUMAN NOD1_HUMAN]] Enhances caspase-9-mediated apoptosis. Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection.<ref>PMID:11058605</ref> <ref>PMID:19043560</ref> <ref>PMID:22672233</ref> <ref>PMID:17054981</ref>
| + | [https://www.uniprot.org/uniprot/NOD1_HUMAN NOD1_HUMAN] Enhances caspase-9-mediated apoptosis. Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection.<ref>PMID:11058605</ref> <ref>PMID:19043560</ref> <ref>PMID:22672233</ref> <ref>PMID:17054981</ref> |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dubas, R L]] | + | [[Category: Dubas RL]] |
| - | [[Category: Park, Y C]] | + | [[Category: Park YC]] |
| - | [[Category: Robbins, S L]] | + | [[Category: Robbins SL]] |
| - | [[Category: Thiagarajan, S]] | + | [[Category: Thiagarajan S]] |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Helix swapped]]
| + | |
| Structural highlights
Function
NOD1_HUMAN Enhances caspase-9-mediated apoptosis. Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection.[1] [2] [3] [4]
Publication Abstract from PubMed
Nod1 is an essential cytoplasmic sensor for bacterial peptidoglycans in the innate immune system. The caspase-recruitment domain of Nod1 (Nod1_CARD) is indispensable for recruiting a downstream kinase, receptor-interacting protein 2 (RIP2), that activates nuclear factor-kappaB (NF-kappaB). The crystal structure of human Nod1_CARD at 1.9 A resolution reveals a novel homodimeric conformation. Our structural and biochemical analysis shows that the homodimerization of Nod1_CARD is achieved by swapping the H6 helices at the carboxy termini and stabilized by forming an interchain disulfide bond between the Cys39 residues of the two monomers in solution and in the crystal. In addition, we present experimental evidence for a pH-sensitive conformational change of Nod1_CARD. Our results suggest that the pH-sensitive monomer/dimer transition is a unique molecular property of Nod1_CARD.
Monomer/dimer transition of the caspase-recruitment domain of human Nod1.,Srimathi T, Robbins SL, Dubas RL, Hasegawa M, Inohara N, Park YC Biochemistry. 2008 Feb 5;47(5):1319-25. Epub 2008 Jan 11. PMID:18186648[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Inohara N, Ogura Y, Chen FF, Muto A, Nunez G. Human Nod1 confers responsiveness to bacterial lipopolysaccharides. J Biol Chem. 2001 Jan 26;276(4):2551-4. Epub 2000 Oct 31. PMID:11058605 doi:10.1074/jbc.M009728200
- ↑ Fukazawa A, Alonso C, Kurachi K, Gupta S, Lesser CF, McCormick BA, Reinecker HC. GEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectors. PLoS Pathog. 2008 Nov;4(11):e1000228. doi: 10.1371/journal.ppat.1000228. Epub, 2008 Nov 28. PMID:19043560 doi:10.1371/journal.ppat.1000228
- ↑ Lautz K, Damm A, Menning M, Wenger J, Adam AC, Zigrino P, Kremmer E, Kufer TA. NLRP10 enhances Shigella-induced pro-inflammatory responses. Cell Microbiol. 2012 Oct;14(10):1568-83. doi: 10.1111/j.1462-5822.2012.01822.x., Epub 2012 Jun 21. PMID:22672233 doi:10.1111/j.1462-5822.2012.01822.x
- ↑ Manon F, Favier A, Nunez G, Simorre JP, Cusack S. Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RICK. J Mol Biol. 2007 Jan 5;365(1):160-74. Epub 2006 Sep 29. PMID:17054981 doi:10.1016/j.jmb.2006.09.067
- ↑ Srimathi T, Robbins SL, Dubas RL, Hasegawa M, Inohara N, Park YC. Monomer/dimer transition of the caspase-recruitment domain of human Nod1. Biochemistry. 2008 Feb 5;47(5):1319-25. Epub 2008 Jan 11. PMID:18186648 doi:10.1021/bi7016602
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