2mjm: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry~~ 2mjm is ~~ON HOLD~~

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

== 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.

== 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.

~~Authors:~~ Gutte, P.G.M., ~~Zerbe, O~~.

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>

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

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

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Mus musculus]]

[[Category: Gutte PGM]]

[[Category: Zerbe O]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2mjm is ON HOLD
+==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.
-Authors: Gutte, P.G.M., Zerbe, O.
+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>
-Description: The solution NMR structure of the NLRC5 caspase recruitment domain (CARD)
+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: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Gutte PGM]]
+[[Category: Zerbe O]]