Unknown

Dataset Information

0

Single particle cryo-EM structure of RIG-I bound to the end and internal sites of OH3SLR30 (+ATP)


ABSTRACT:

SUBMITTER: Anna Marie Pyle 

PROVIDER: EMPIAR-11332 | biostudies-other |

REPOSITORIES: biostudies-other

altmetric image

Publications

The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands.

Wang Wenshuai W   Pyle Anna Marie AM  

Molecular cell 20221021 21


RIG-I is an essential innate immune receptor for detecting and responding to infection by RNA viruses. RIG-I specifically recognizes the unique molecular features of viral RNA molecules and selectively distinguishes them from closely related RNAs abundant in host cells. The physical basis for this exquisite selectivity is revealed through a series of high-resolution cryo-EM structures of RIG-I in complex with host and viral RNA ligands. These studies demonstrate that RIG-I actively samples doubl  ...[more]

Similar Datasets

| EMPIAR-11328 | biostudies-other
| EMPIAR-11337 | biostudies-other
| EMPIAR-11326 | biostudies-other
| EMPIAR-11329 | biostudies-other
| EMPIAR-11330 | biostudies-other
| EMPIAR-11331 | biostudies-other
| EMPIAR-11494 | biostudies-other
| EMPIAR-11496 | biostudies-other
| S-EPMC6009202 | biostudies-literature
| S-EPMC7611073 | biostudies-literature