Author: Brisse, Morgan; Ly, Hinh
Title: Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 Document date: 2019_7_17
ID: 1enteev7_34
Snippet: As previously mentioned, MDA5 preferentially associates with long dsRNA (76) (77) (78) (79) . The crystal structure and molecular modeling of MDA5/dsRNA complex suggest that it can recognize the entire first turn of the blunt-ended dsRNA (182) in a similar way as LGP2 can (183) . Like RIG-I and MDA5, LGP2 belongs to the ATP-dependent DExD/H box RNA helicases (184) , which is structurally similar to RIG-I and MDA5 but lacks the CARD domains at the.....
Document: As previously mentioned, MDA5 preferentially associates with long dsRNA (76) (77) (78) (79) . The crystal structure and molecular modeling of MDA5/dsRNA complex suggest that it can recognize the entire first turn of the blunt-ended dsRNA (182) in a similar way as LGP2 can (183) . Like RIG-I and MDA5, LGP2 belongs to the ATP-dependent DExD/H box RNA helicases (184) , which is structurally similar to RIG-I and MDA5 but lacks the CARD domains at the N terminus (185) . MDA5 has also been found to be activated by the digested products of RNase L specifically from parainfluenza virus (186) .
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