5wwg
Crystal structure of hnRNPA2B1 in complex with AAGGACUUGC
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 PubMedHuman hnRNP A2/B1 is an RNA-binding protein that plays important roles in many biological processes, including maturation, transport, and metabolism of mRNA, and gene regulation of long noncoding RNAs. hnRNP A2/B1 was reported to control the microRNAs sorting to exosomes and promote primary microRNA processing as a potential m(6)A "reader." hnRNP A2/B1 contains two RNA recognition motifs that provide sequence-specific recognition of RNA substrates. Here, we determine crystal structures of tandem RRM domains of hnRNP A2/B1 in complex with various RNA substrates, elucidating specific recognitions of AGG and UAG motifs by RRM1 and RRM2 domains, respectively. Further structural and biochemical results demonstrate multivariant binding modes for sequence-diversified RNA substrates, supporting a RNA matchmaker mechanism in hnRNP A2/B1 function. Moreover, our studies in combination with bioinformatic analysis suggest that hnRNP A2/B1 may mediate effects of m(6)A through a "m(6)A switch" mechanism, instead of acting as a direct "reader" of m(6)A modification. Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1.,Wu B, Su S, Patil DP, Liu H, Gan J, Jaffrey SR, Ma J Nat Commun. 2018 Jan 29;9(1):420. doi: 10.1038/s41467-017-02770-z. PMID:29379020[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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