4AY2

Capturing 5' tri-phosphorylated RNA duplex by RIG-I

Summary for 4AY2

• Entry DOI: 10.2210/pdb4ay2/pdb
• Related: 2YKG
• Descriptor: PROBABLE ATP-DEPENDENT RNA HELICASE DDX58, 5'-R-PPP(GP*GP*CP*GP*CP*GP*GP*CP*UP*UP*CP*GP*GP*CP *CP*GP*CP*GP*CP*C)-3', ZINC ION, ... (6 entities in total)
• Functional Keywords: hydrolase-rna complex, innate immunity, hydrolase/rna
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: O95786
• Total number of polymer chains: 2
• Total formula weight: 85784.49

Authors

Luo, D.,Pyle, A.M. (deposition date: 2012-06-17, release date: 2012-10-03, Last modification date: 2024-10-09)

Primary citation

Luo, D.,Kohlway, A.,Vela, A.,Pyle, A.M.
Visualizing the Determinants of Viral RNA Recognition by Innate Immune Sensor Rig-I.
Structure, 20:1983-, 2012

PubMed Abstract: Retinoic acid inducible gene-I (RIG-I) is a key intracellular immune receptor for pathogenic RNAs, particularly from RNA viruses. Here, we report the crystal structure of human RIG-I bound to a 5' triphosphorylated RNA hairpin and ADP nucleotide at 2.8 Å resolution. The RNA ligand contains all structural features that are essential for optimal recognition by RIG-I, as it mimics the panhandle-like signatures within the genome of negative-stranded RNA viruses. RIG-I adopts an intermediate, semiclosed conformation in this product state of ATP hydrolysis. The structure of this complex allows us to visualize the first steps in RIG-I recognition and activation upon viral infection.

PubMed: 23022350
DOI: 10.1016/J.STR.2012.08.029

Experimental method

X-RAY DIFFRACTION (2.8 Å)