RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner.
Peisley, Alys; Wu, Bin; Yao, Hui; Walz, Thomas; Hur, Sun.
; 51(5): 573-83, 2013 Sep 12.
Artigo em Inglês | MEDLINE | ID: mdl-23993742
Structural insights into RNA recognition by RIG-I.
Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5.
The DEAD-box protein DDX43 (HAGE) is a dual RNA-DNA helicase and has a K-homology domain required for full nucleic acid unwinding activity.
Structural mechanism of RNA recognition by the RIG-I-like receptors.
The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly.
MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA.
Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5.
ATP-dependent effector-like functions of RIG-I-like receptors.
Repetitive RNA unwinding by RNA helicase A facilitates RNA annealing.
A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivo.