5HO4

Crystal structure of hnRNPA2B1 in complex with 10-mer RNA

Summary for 5HO4

• Entry DOI: 10.2210/pdb5ho4/pdb
• Descriptor: Heterogeneous nuclear ribonucleoproteins A2/B1, RNA (5'-R(*AP*AP*GP*GP*AP*CP*UP*AP*GP*C)-3') (3 entities in total)
• Functional Keywords: hnrnpa2b1, rrms, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 23758.18

Authors

Wu, B.X.,Su, S.C.,Gan, J.H.,Ma, J.B. (deposition date: 2016-01-19, release date: 2017-02-08, Last modification date: 2024-03-20)

Primary citation

Wu, B.X.,Su, S.C.,Patil, D.P.,Liu, H.,Gan, J.H.,Jaffrey, S.R.,Ma, J.B.
Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1.
Nat Commun, 9:420-420, 2018

PubMed Abstract: Human 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 mA "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 mA through a "mA switch" mechanism, instead of acting as a direct "reader" of mA modification.

PubMed: 29379020
DOI: 10.1038/s41467-017-02770-z

Experimental method

X-RAY DIFFRACTION (1.85 Å)