Abstract:
:Heterogeneous nuclear ribonucleoproteins (hnRNPs) can be divided into subgroups based on their RNA-binding characteristics. One subgroup in mammalian cells are the Poly(C)-binding proteins (PCBPs) comprised of hnRNP K/J and hnRNP E1-4 [the latter also known as PCBP 1-4 or α-complex proteins (α-CP) 1-4]. Each subgroup member has three K homology (KH) nucleic acid-binding domains. Individual KH domains bind short single-stranded (ss), poly-pyrimidine-rich nucleic acid sequences with rather weak affinity. In this study, we report the (1)H, (13)C and (15)N backbone resonance assignments of the first and second KH domains of hnRNP E1, which plays a pivotal role in posttranscriptional and translational regulation of RNA targets. Our NMR assignments lay the foundation for a detailed investigation of the dynamic cooperation of the tandem KH1 and KH2 domains to bind nucleic acids.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Li Y,Hennig Mdoi
10.1007/s12104-015-9624-0subject
Has Abstractpub_date
2015-10-01 00:00:00pages
431-4issue
2eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-015-9624-0journal_volume
9pub_type
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