4h22
From Proteopedia
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| - | [[ | + | ==Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1== |
| + | <StructureSection load='4h22' size='340' side='right' caption='[[4h22]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4h22]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H22 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q6q|2q6q]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LRRFIP1, GCF2, TRIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4h22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h22 RCSB], [http://www.ebi.ac.uk/pdbsum/4h22 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | LRRFIP1 binds cytoplasmic double-stranded DNA and RNA and interacts with FLI, the mammalian homolog of Drosophila flightless I, through a highly conserved 87-amino acid domain. Upon binding nucleic acid ligands, LRRFIP1 recruits and activates beta-catenin, leading to the IRF3-dependent production of type I interferon. However, the molecular mechanism of LRRFIP1 signaling is not well understood. Here we show that the FLI-interacting domain of LRRFIP1 forms a classic parallel, homodimeric coiled coil with 10 heptad repeats and 22 helical turns. The coiled coil domain is also a dimer in solution. However, a longer LRRFIP1 construct spanning the coiled coil and DNA binding domains assembles into higher order oligomers in solution. The structure of LRRFIP1-CC constitutes a valuable tool for probing the mechanism of LRRFIP1 signaling and for structural studies of larger LRRFIP1 constructs. | ||
| - | + | Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1.,Nguyen JB, Modis Y J Struct Biol. 2012 Oct 23. pii: S1047-8477(12)00274-2. doi:, 10.1016/j.jsb.2012.10.006. PMID:23099021<ref>PMID:23099021</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Modis, Y | + | [[Category: Modis, Y]] |
| - | [[Category: Nguyen, J B | + | [[Category: Nguyen, J B]] |
[[Category: Flightless-1]] | [[Category: Flightless-1]] | ||
[[Category: Nucleic acid sensor]] | [[Category: Nucleic acid sensor]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
Revision as of 09:57, 10 December 2014
Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1
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