3ZD7
Snapshot 3 of RIG-I scanning on RNA duplex
Summary for 3ZD7
Entry DOI | 10.2210/pdb3zd7/pdb |
Related | 3ZD6 |
Descriptor | PROBABLE ATP-DEPENDENT RNA HELICASE DDX58, RNA DUPLEX, ZINC ION, ... (6 entities in total) |
Functional Keywords | hydrolase-rna complex, helicase, innate immunity, hydrolase/rna |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Cytoplasm: O95786 |
Total number of polymer chains | 3 |
Total formula weight | 86642.67 |
Authors | Luo, D.,Pyle, A.M. (deposition date: 2012-11-25, release date: 2013-08-07, Last modification date: 2023-12-20) |
Primary citation | Kohlway, A.,Luo, D.,Rawling, D.C.,Ding, S.C.,Pyle, A.M. Defining the Functional Determinants for RNA Surveillance by Rig-I. Embo Rep., 14:772-, 2013 Cited by PubMed Abstract: Retinoic acid-inducible gene-I (RIG-I) is an intracellular RNA sensor that activates the innate immune machinery in response to infection by RNA viruses. Here, we report the crystal structure of distinct conformations of a RIG-I:dsRNA complex, which shows that HEL2i-mediated scanning allows RIG-I to sense the length of RNA targets. To understand the implications of HEL2i scanning for catalytic activity and signalling by RIG-I, we examined its ATPase activity when stimulated by duplex RNAs of varying lengths and 5' composition. We identified a minimal RNA duplex that binds one RIG-I molecule, stimulates robust ATPase activity, and elicits a RIG-I-mediated interferon response in cells. Our results reveal that the minimal functional unit of the RIG-I:RNA complex is a monomer that binds at the terminus of a duplex RNA substrate. This behaviour is markedly different from the RIG-I paralog melanoma differentiation-associated gene 5 (MDA5), which forms cooperative filaments. PubMed: 23897087DOI: 10.1038/EMBOR.2013.108 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report