|
|
| Line 1: |
Line 1: |
| | | | |
| | ==The solution NMR structure of the NLRC5 caspase recruitment domain (CARD)== | | ==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 == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mjm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nlrc5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </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> |
| - | <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> | | </table> |
| | == Function == | | == 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.
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gutte, P G.M]] | + | [[Category: Gutte PGM]] |
| - | [[Category: Zerbe, O]] | + | [[Category: Zerbe O]] |
| - | [[Category: Card]]
| + | |
| - | [[Category: Death fold]]
| + | |
| - | [[Category: Inflammation]]
| + | |
| - | [[Category: Innate immune system]]
| + | |
| - | [[Category: Nlrc5]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| - | [[Category: Rig-i]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
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
|
