5irm: Difference between revisions
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<StructureSection load='5irm' size='340' side='right'caption='[[5irm]], [[Resolution|resolution]] 3.31Å' scene=''> | <StructureSection load='5irm' size='340' side='right'caption='[[5irm]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5irm]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5irm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IRM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.31Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5irm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5irm OCA], [https://pdbe.org/5irm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5irm RCSB], [https://www.ebi.ac.uk/pdbsum/5irm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5irm ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G1T469_RABIT G1T469_RABIT] | |||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Oryctolagus cuniculus]] | ||
[[Category: | [[Category: Maekawa S]] | ||
[[Category: | [[Category: Ohto U]] | ||
[[Category: | [[Category: Shimizu T]] | ||
Revision as of 17:07, 30 August 2023
Crystal structure of rabbit NOD2 in an ADP-bound state (Crystal form2)Crystal structure of rabbit NOD2 in an ADP-bound state (Crystal form2)
Structural highlights
FunctionPublication Abstract from PubMedNucleotide-binding oligomerization domain-containing protein 2 (NOD2), a member of the NOD-like receptors family, are crucial for innate immune responses. Mutations of NOD2 have been associated with chronic inflammatory disorders such as Crohn's disease (CD), Blau syndrome (BS) and early-onset sarcoidosis (EOS), but little is known about its signalling mechanism and the role it plays in these diseases. Here, we report the crystal structure of rabbit NOD2 in an ADP-bound state. The structure reveals an inactive closed conformation in which the subdomains in the NOD domain are closely packed by ADP-mediated and inter-domain interactions. Mapping of the BS- or EOS-associated gain-of-function mutations reveals that most of these mutations are located in the NOD subdomain interfaces, and are likely to disrupt the inner domain interactions, facilitating a conformational change to the active form. Conversely, mutations associated with CD are distributed throughout the protein, some of which may affect oligomer formation and ligand binding. Crystal structure of NOD2 and its implications in human disease.,Maekawa S, Ohto U, Shibata T, Miyake K, Shimizu T Nat Commun. 2016 Jun 10;7:11813. doi: 10.1038/ncomms11813. PMID:27283905[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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