Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands.
Journal, issue, pages	Mol Cell, Vol. 82, Issue 21, Page 4131-44144.e6, Year 2022
Publish date	Nov 3, 2022
Authors	Wenshuai Wang / Anna Marie Pyle /
PubMed Abstract	RIG-I is an essential innate immune receptor for detecting and responding to infection by RNA viruses. RIG-I specifically recognizes the unique molecular features of viral RNA molecules and ...RIG-I is an essential innate immune receptor for detecting and responding to infection by RNA viruses. RIG-I specifically recognizes the unique molecular features of viral RNA molecules and selectively distinguishes them from closely related RNAs abundant in host cells. The physical basis for this exquisite selectivity is revealed through a series of high-resolution cryo-EM structures of RIG-I in complex with host and viral RNA ligands. These studies demonstrate that RIG-I actively samples double-stranded RNAs in the cytoplasm and distinguishes them by adopting two different types of protein folds. Upon binding viral RNA, RIG-I adopts a high-affinity conformation that is conducive to signaling, while host RNA induces an autoinhibited conformation that stimulates RNA release. By coupling protein folding with RNA binding selectivity, RIG-I distinguishes RNA molecules that differ by as little as one phosphate group, thereby explaining the molecular basis for selective antiviral sensing and the induction of autoimmunity upon RIG-I dysregulation.
External links	Mol Cell / PubMed:36272408 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.66 Å
Structure data	26022 7tnx EMDB-26022, PDB-7tnx: Cryo-EM structure of RIG-I in complex with p3dsRNA Method: EM (single particle) / Resolution: 3.54 Å 26023 7tny EMDB-26023, PDB-7tny: Cryo-EM structure of RIG-I in complex with p2dsRNA Method: EM (single particle) / Resolution: 3.2 Å 26024 7tnz EMDB-26024, PDB-7tnz: Cryo-EM structure of RIG-I in complex with p1dsRNA Method: EM (single particle) / Resolution: 3.54 Å 26025 7to0 EMDB-26025, PDB-7to0: Cryo-EM structure of RIG-I in complex with OHdsRNA Method: EM (single particle) / Resolution: 3.5 Å 26026 7to1 EMDB-26026, PDB-7to1: Cryo-EM structure of RIG-I bound to the end of p3SLR30 (+ATP) Method: EM (single particle) / Resolution: 3.66 Å 26027 7to2 EMDB-26027, PDB-7to2: Cryo-EM structure of RIG-I bound to the internal sites of p3SLR30 (+ATP) Method: EM (single particle) / Resolution: 3.2 Å 27743 8dvr EMDB-27743, PDB-8dvr: Cryo-EM structure of RIG-I bound to the end of p3SLR30 (+AMPPNP) Method: EM (single particle) / Resolution: 3.3 Å 27744 8dvs EMDB-27744, PDB-8dvs: Cryo-EM structure of RIG-I bound to the end of OHSLR30 (+ATP) Method: EM (single particle) / Resolution: 3.0 Å 27745 8dvu EMDB-27745, PDB-8dvu: Cryo-EM structure of RIG-I bound to the internal sites of OHSLR30 (+ATP) Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM
Source	homo sapiens (human)
Keywords	IMMUNE SYSTEM/RNA / ribonucleoprotein complex / RNA sensor / RIG-I like receptor / IMMUNE SYSTEM / IMMUNE SYSTEM-RNA complex / Hydrolase/RNA / Hydrolase-RNA complex