Summary information and primary citation
- PDB-id
- 7wm3; DSSR-derived features in text and JSON formats
- Class
- DNA binding protein-DNA
- Method
- X-ray (1.62 Å)
- Summary
- Hnrnp a2-b1 rrms in complex with single-stranded DNA
- Reference
- Liu Y, Abula A, Xiao H, Guo H, Li T, Zheng L, Chen B, Nguyen HC, Ji X (2022): "Structural Insight Into hnRNP A2/B1 Homodimerization and DNA Recognition." J.Mol.Biol., 435, 167920. doi: 10.1016/j.jmb.2022.167920.
- Abstract
- Heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) has been identified as a nuclear DNA sensor. Upon viral infection, hnRNP A2/B1 recognizes pathogen-derived DNA as a homodimer, which is a prerequisite for its translocation to the cytoplasm to activate the interferon response. However, the DNA binding mechanism inducing hnRNP A2/B1 homodimerization is unknown. Here, we show the crystal structure of the RNA recognition motif (RRM) of hnRNP A2/B1 in complex with a U-shaped ssDNA, which mediates the formation of a newly observed protein dimer. Our biochemical assays and mutagenesis studies confirm that the hnRNP A2/B1 homodimer forms in solution by binding to pre-generated ssDNA or dsDNA with a U-shaped bulge. These results depict a potential functional state of hnRNP A2/B1 in antiviral immunity and other cellular processes.
