4H22
Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1
Summary for 4H22
| Entry DOI | 10.2210/pdb4h22/pdb |
| Related | 2q6q |
| Descriptor | Leucine-rich repeat flightless-interacting protein 1 (2 entities in total) |
| Functional Keywords | nucleic acid sensor, flightless-1, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q32MZ4 |
| Total number of polymer chains | 4 |
| Total formula weight | 49599.78 |
| Authors | Nguyen, J.B.,Modis, Y. (deposition date: 2012-09-11, release date: 2012-11-07, Last modification date: 2023-09-20) |
| Primary citation | Nguyen, J.B.,Modis, Y. Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1. J.Struct.Biol., 181:82-88, 2013 Cited by PubMed Abstract: 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 β-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. PubMed: 23099021DOI: 10.1016/j.jsb.2012.10.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.89 Å) |
Structure validation
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