2mjm: Difference between revisions
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The | ==The solution NMR structure of the NLRC5 caspase recruitment domain (CARD)== | ||
<StructureSection load='2mjm' size='340' side='right'caption='[[2mjm]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mjm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjm OCA], [https://pdbe.org/2mjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mjm RCSB], [https://www.ebi.ac.uk/pdbsum/2mjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NLRC5_MOUSE NLRC5_MOUSE] Probable regulator of the NF-kappa-B and type I interferon signaling pathways. May also regulate the type II interferon signaling pathway. Plays a role in homeostatic control of innate immunity and in antiviral defense mechanisms. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cytosolic nucleotide-binding domain and leucine-rich repeat-containing receptors (NLRs) are key sensors for bacterial and viral invaders and endogenous stress signals. NLRs contain a varying N-terminal effector domain that regulates the downstream signaling events upon its activation and determines the subclass to which a NLR member belongs. NLRC5 contains an unclassified N-terminal effector domain that has been reported to interact downstream with the tandem caspase recruitment domain (CARD) of retinoic acid-inducible gene I (RIG-I). Here we report the solution structure of the N-terminal effector domain of NLRC5 and in vitro interaction experiments with the tandem CARD of RIG-I. The N-terminal effector domain of NLRC5 adopts a six alpha-helix bundle with a general death fold, though it displays specific structural features that are strikingly different from the CARD. Notably, alpha-helix 3 is replaced by an ordered loop, and alpha-helix 1 is devoid of the characteristic interruption. Detailed structural alignments between the N-terminal effector domains of NLRC5 with a representative of each death-fold subfamily showed that NLRC5 fits best to the CARD subfamily and can be called an atypical CARD. Due to the specific structural features, the atypical CARD also displays a different electrostatic surface. Because the shape and charge of the surface is crucial for the establishment of a homotypic CARD-CARD interaction, these specific structural features seem to have a significant effect on the interaction between the atypical CARD of NLRC5 and the tandem RIG-I CARD. | |||
Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.,Gutte PG, Jurt S, Grutter MG, Zerbe O Biochemistry. 2014 May 20;53(19):3106-17. doi: 10.1021/bi500177x. Epub 2014 May, 9. PMID:24815518<ref>PMID:24815518</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2mjm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Gutte PGM]] | |||
[[Category: Zerbe O]] | |||
