2RMJ

Solution structure of RIG-I C-terminal domain

Summary for 2RMJ

• Entry DOI: 10.2210/pdb2rmj/pdb
• Descriptor: Probable ATP-dependent RNA helicase DDX58 (1 entity in total)
• Functional Keywords: rna binding protein, alternative splicing, antiviral defense, atp-binding, cytoplasm, helicase, hydrolase, immune response, innate immunity, interferon induction, nucleotide-binding, polymorphism, rna-binding, ubl conjugation
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O95786
• Total number of polymer chains: 1
• Total formula weight: 15659.18

Authors

Takahasi, K.,Yoneyama, M.,Nihishori, T.,Hirai, R.,Narita, R.,Gale Jr., M.,Fujita, T.,Inagaki, F. (deposition date: 2007-10-23, release date: 2008-03-25, Last modification date: 2024-05-29)

Primary citation

Takahasi, K.,Yoneyama, M.,Nishihori, T.,Hirai, R.,Kumeta, H.,Narita, R.,Gale Jr., M.,Inagaki, F.,Fujita, T.
Nonself RNA-Sensing Mechanism of RIG-I Helicase and Activation of Antiviral Immune Responses
Mol.Cell, 29:428-440, 2008

PubMed Abstract: A DExD/H protein, RIG-I, is critical in innate antiviral responses by sensing viral RNA. Here we show that RIG-I recognizes two distinct viral RNA patterns: double-stranded (ds) and 5'ppp single-stranded (ss) RNA. The binding of RIG-I with dsRNA or 5'ppp ssRNA in the presence of ATP produces a common structure, as suggested by protease digestion. Further analyses demonstrated that the C-terminal domain of RIG-I (CTD) recognizes these RNA patterns and CTD coincides with the autorepression domain. Structural analysis of CTD by NMR spectroscopy in conjunction with mutagenesis revealed that the basic surface of CTD with a characteristic cleft interacts with RIG-I ligands. Our results suggest that the bipartite structure of CTD regulates RIG-I on encountering viral RNA patterns.

PubMed: 18242112
DOI: 10.1016/j.molcel.2007.11.028

Experimental method

SOLUTION NMR