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PDBsum entry 2ykg
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References listed in PDB file
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Key reference
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Title
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Structural insights into RNA recognition by rig-I.
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Authors
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D.Luo,
S.C.Ding,
A.Vela,
A.Kohlway,
B.D.Lindenbach,
A.M.Pyle.
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Ref.
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Cell, 2011,
147,
409-422.
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PubMed id
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Abstract
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Intracellular RIG-I-like receptors (RLRs, including RIG-I, MDA-5, and LGP2)
recognize viral RNAs as pathogen-associated molecular patterns (PAMPs) and
initiate an antiviral immune response. To understand the molecular basis of this
process, we determined the crystal structure of RIG-I in complex with
double-stranded RNA (dsRNA). The dsRNA is sheathed within a network of protein
domains that include a conserved "helicase" domain (regions HEL1 and
HEL2), a specialized insertion domain (HEL2i), and a C-terminal regulatory
domain (CTD). A V-shaped pincer connects HEL2 and the CTD by gripping an
α-helical shaft that extends from HEL1. In this way, the pincer coordinates
functions of all the domains and couples RNA binding with ATP hydrolysis. RIG-I
falls within the Dicer-RIG-I clade of the superfamily 2 helicases, and this
structure reveals complex interplay between motor domains, accessory mechanical
domains, and RNA that has implications for understanding the nanomechanical
function of this protein family and other ATPases more broadly.
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