8DVU

Cryo-EM structure of RIG-I bound to the internal sites of OHSLR30 (+ATP)

Summary for 8DVU

• Entry DOI: 10.2210/pdb8dvu/pdb
• EMDB information: 27745
• Descriptor: Antiviral innate immune response receptor RIG-I, OHSLR30, ZINC ION, ... (5 entities in total)
• Functional Keywords: ribonucleoprotein complex, rna sensor, rig-i like receptor, hydrolase-rna complex, hydrolase/rna
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 127806.67

Authors

Wang, W.,Pyle, A.M. (deposition date: 2022-07-29, release date: 2022-11-16, Last modification date: 2024-06-12)

Primary citation

Wang, W.,Pyle, A.M.
The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands.
Mol.Cell, 82:4131-4144.e6, 2022

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 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.

PubMed: 36272408
DOI: 10.1016/j.molcel.2022.09.029

Experimental method

ELECTRON MICROSCOPY (2.9 Å)