4h22: Difference between revisions

Revision as of 07:54, 3 November 2022

Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1

Structural highlights

4h22 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5]

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^[6]

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

References

↑ Khachigian LM, Santiago FS, Rafty LA, Chan OL, Delbridge GJ, Bobik A, Collins T, Johnson AC. GC factor 2 represses platelet-derived growth factor A-chain gene transcription and is itself induced by arterial injury. Circ Res. 1999 Jun 11;84(11):1258-67. PMID:10364563
↑ Rikiyama T, Curtis J, Oikawa M, Zimonjic DB, Popescu N, Murphy BA, Wilson MA, Johnson AC. GCF2: expression and molecular analysis of repression. Biochim Biophys Acta. 2003 Oct 1;1629(1-3):15-25. PMID:14522076
↑ Suriano AR, Sanford AN, Kim N, Oh M, Kennedy S, Henderson MJ, Dietzmann K, Sullivan KE. GCF2/LRRFIP1 represses tumor necrosis factor alpha expression. Mol Cell Biol. 2005 Oct;25(20):9073-81. PMID:16199883 doi:https://dx.doi.org/25/20/9073
↑ Dai P, Jeong SY, Yu Y, Leng T, Wu W, Xie L, Chen X. Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins. J Immunol. 2009 Mar 15;182(6):3450-60. doi: 10.4049/jimmunol.0802260. PMID:19265123 doi:https://dx.doi.org/10.4049/jimmunol.0802260
↑ Reed AL, Yamazaki H, Kaufman JD, Rubinstein Y, Murphy B, Johnson AC. Molecular cloning and characterization of a transcription regulator with homology to GC-binding factor. J Biol Chem. 1998 Aug 21;273(34):21594-602. PMID:9705290
↑ Nguyen JB, Modis Y. Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1. J Struct Biol. 2012 Oct 23. pii: S1047-8477(12)00274-2. doi:, 10.1016/j.jsb.2012.10.006. PMID:23099021 doi:https://dx.doi.org/10.1016/j.jsb.2012.10.006

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Khachigian LM, Santiago FS, Rafty LA, Chan OL, Delbridge GJ, Bobik A, Collins T, Johnson AC. GC factor 2 represses platelet-derived growth factor A-chain gene transcription and is itself induced by arterial injury. Circ Res. 1999 Jun 11;84(11):1258-67. PMID:10364563

[2] Rikiyama T, Curtis J, Oikawa M, Zimonjic DB, Popescu N, Murphy BA, Wilson MA, Johnson AC. GCF2: expression and molecular analysis of repression. Biochim Biophys Acta. 2003 Oct 1;1629(1-3):15-25. PMID:14522076

[3] Suriano AR, Sanford AN, Kim N, Oh M, Kennedy S, Henderson MJ, Dietzmann K, Sullivan KE. GCF2/LRRFIP1 represses tumor necrosis factor alpha expression. Mol Cell Biol. 2005 Oct;25(20):9073-81. PMID:16199883 doi:https://dx.doi.org/25/20/9073

[4] Dai P, Jeong SY, Yu Y, Leng T, Wu W, Xie L, Chen X. Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins. J Immunol. 2009 Mar 15;182(6):3450-60. doi: 10.4049/jimmunol.0802260. PMID:19265123 doi:https://dx.doi.org/10.4049/jimmunol.0802260

[5] Reed AL, Yamazaki H, Kaufman JD, Rubinstein Y, Murphy B, Johnson AC. Molecular cloning and characterization of a transcription regulator with homology to GC-binding factor. J Biol Chem. 1998 Aug 21;273(34):21594-602. PMID:9705290

[6] Nguyen JB, Modis Y. Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1. J Struct Biol. 2012 Oct 23. pii: S1047-8477(12)00274-2. doi:, 10.1016/j.jsb.2012.10.006. PMID:23099021 doi:https://dx.doi.org/10.1016/j.jsb.2012.10.006

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
 ==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]] 2.89&Aring;' scene=''>
+<StructureSection load='4h22' size='340' side='right'caption='[[4h22]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4h22]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q6q|2q6q]]</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=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>
-<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 HUMAN])</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://pdbe.org/4h22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h22 RCSB], [http://www.ebi.ac.uk/pdbsum/4h22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h22 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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 ==
@@ Line 23: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Modis, Y]]
+[[Category: Large Structures]]
-[[Category: Nguyen, J B]]
+[[Category: Modis Y]]
-[[Category: Flightless-1]]
+[[Category: Nguyen JB]]
-[[Category: Nucleic acid sensor]]
-[[Category: Transcription]]

4h22: Difference between revisions

Revision as of 07:54, 3 November 2022

Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools