Article
Molecular basis for PKR activation by PACT or dsRNA.
Proceedings of the National Academy of Sciences of the United States of America - 27 Jun 2006
Li Shoudong, Peters Gregory A, Ding Keyang, Zhang Xiaolun, Qin Jun, Sen Ganes C
Abstract excerpt
The mammalian protein kinase PKR is a critical component of the innate immune response against virus infection. Its cellular actions are mediated by modulating cell signaling and translational regulation. To be enzymatically active, latent PKR needs to be activated by binding to one of its activators, dsRNA or PACT protein. Although the structures of the N-terminal dsRNA-binding domain and the C-terminal kinase...
Topics
- Amino Acid Motifs
- Cells, Cultured
- Enzyme Activation
- Humans
- Mutation
- Nuclear Magnetic Resonance, Biomolecular
- Nuclear Proteins
- Peptides
- Protein Interaction Mapping
- Protein Structure, Tertiary
- RNA, Double-Stranded
- RNA-Binding Proteins
- eIF-2 Kinase