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4h22
From Proteopedia
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| - | [[Image:4h22.png|left|200px]] | ||
| - | + | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4H22 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.89Å</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=4h22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h22 OCA], [https://pdbe.org/4h22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h22 RCSB], [https://www.ebi.ac.uk/pdbsum/4h22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h22 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LRRF1_HUMAN LRRF1_HUMAN] Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding.<ref>PMID:10364563</ref> <ref>PMID:14522076</ref> <ref>PMID:16199883</ref> <ref>PMID:19265123</ref> <ref>PMID:9705290</ref> | ||
| + | <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> | |
| - | == | + | <div class="pdbe-citations 4h22" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Modis Y]] |
| - | [[Category: | + | [[Category: Nguyen JB]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1
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