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2mjm

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The solution NMR structure of the NLRC5 caspase recruitment domain (CARD)

Structural highlights

2mjm is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gutte PG, Jurt S, Grutter MG, Zerbe O. Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain. Biochemistry. 2014 May 20;53(19):3106-17. doi: 10.1021/bi500177x. Epub 2014 May, 9. PMID:24815518 doi:http://dx.doi.org/10.1021/bi500177x

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mjm"

Categories: Large Structures | Mus musculus | Gutte PGM | Zerbe O

@@ Line 1: / Line 1: @@
 ==The solution NMR structure of the NLRC5 caspase recruitment domain (CARD)==
-<StructureSection load='2mjm' size='340' side='right' caption='[[2mjm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2mjm' size='340' side='right'caption='[[2mjm]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mjm]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MJM FirstGlance]. <br>
+<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='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=2mjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mjm RCSB], [http://www.ebi.ac.uk/pdbsum/2mjm PDBsum]</span></td></tr>
+</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 ==
-[[http://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.
+[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 ==
@@ Line 15: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, 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: Gutte, P G.M]]
+[[Category: Large Structures]]
-[[Category: Zerbe, O]]
+[[Category: Mus musculus]]
-[[Category: Card]]
+[[Category: Gutte PGM]]
-[[Category: Death fold]]
+[[Category: Zerbe O]]
-[[Category: Inflammation]]
-[[Category: Innate immune system]]
-[[Category: Nlrc5]]
-[[Category: Protein binding]]
-[[Category: Protein-protein interaction]]
-[[Category: Rig-i]]
-[[Category: Signaling protein]]

2mjm

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Current revision

The solution NMR structure of the NLRC5 caspase recruitment domain (CARD)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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