View source for 2nz7


==Crystal Structure Analysis of Caspase-recruitment Domain (CARD) of Nod1==
<StructureSection load='2nz7' size='340' side='right'caption='[[2nz7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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>
== 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> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:18186648</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2nz7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dubas RL]]
[[Category: Park YC]]
[[Category: Robbins SL]]
[[Category: Thiagarajan S]]