7wm3 | pdb_00007wm3
hnRNP A2/B1 RRMs in complex with single-stranded DNA
Structural highlights
DiseaseROA2_HUMAN Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.[1] FunctionROA2_HUMAN Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Publication Abstract from PubMedHeterogeneous 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. Structural Insight Into hnRNP A2/B1 Homodimerization and DNA Recognition.,Liu Y, Abula A, Xiao H, Guo H, Li T, Zheng L, Chen B, Nguyen HC, Ji X J Mol Biol. 2022 Dec 14;435(3):167920. doi: 10.1016/j.jmb.2022.167920. PMID:36528084[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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