Ontology highlight
ABSTRACT:
SUBMITTER: Xu X
PROVIDER: S-EPMC8421151 | biostudies-literature | 2021 Sep
REPOSITORIES: biostudies-literature
Xu Xinzhou X Zhang Lu L Chu Julie Tung Sem JTS Wang Yuqing Y Chin Alex Wing Hong AWH Chong Tin Hang TH Dai Zixi Z Poon Leo Lit Man LLM Cheung Peter Pak-Hang PP Huang Xuhui X
Nucleic acids research 20210901 15
During RNA elongation, the influenza A viral (IAV) RNA-dependent RNA polymerase (RdRp) residues in the active site interact with the triphosphate moiety of nucleoside triphosphate (NTP) for catalysis. The molecular mechanisms by which they control the rate and fidelity of NTP incorporation remain elusive. Here, we demonstrated through enzymology, virology and computational approaches that the R239 and K235 in the PB1 subunit of RdRp are critical to controlling the activity and fidelity of transc ...[more]