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6Y4H

Solution structure of cold-shock domain 7 and 8 of drosophila Upstream of N-Ras (Unr)

Summary for 6Y4H
Entry DOI10.2210/pdb6y4h/pdb
NMR InformationBMRB: 34492
DescriptorUpstream of N-ras, isoform A (1 entity in total)
Functional Keywordscsd, nccsd, rna binding protein
Biological sourceDrosophila melanogaster (Fruit fly)
Total number of polymer chains1
Total formula weight18672.95
Authors
Hollmann, N.M.,Simon, B.,Hennig, J. (deposition date: 2020-02-21, release date: 2020-07-29, Last modification date: 2024-06-19)
Primary citationHollmann, N.M.,Jagtap, P.K.A.,Masiewicz, P.,Guitart, T.,Simon, B.,Provaznik, J.,Stein, F.,Haberkant, P.,Sweetapple, L.J.,Villacorta, L.,Mooijman, D.,Benes, V.,Savitski, M.M.,Gebauer, F.,Hennig, J.
Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras.
Cell Rep, 32:107930-107930, 2020
Cited by
PubMed Abstract: RNA-binding proteins (RBPs) commonly feature multiple RNA-binding domains (RBDs), which provide these proteins with a modular architecture. Accumulating evidence supports that RBP architectural modularity and adaptability define the specificity of their interactions with RNA. However, how multiple RBDs recognize their cognate single-stranded RNA (ssRNA) sequences in concert remains poorly understood. Here, we use Upstream of N-Ras (Unr) as a model system to address this question. Although reported to contain five ssRNA-binding cold-shock domains (CSDs), we demonstrate that Unr includes an additional four CSDs that do not bind RNA (pseudo-RBDs) but are involved in mediating RNA tertiary structure specificity by reducing the conformational heterogeneity of Unr. Disrupting the interactions between canonical and non-canonical CSDs impacts RNA binding, Unr-mediated translation regulation, and the Unr-dependent RNA interactome. Taken together, our studies reveal a new paradigm in protein-RNA recognition, where interactions between RBDs and pseudo-RBDs select RNA tertiary structures, influence RNP assembly, and define target specificity.
PubMed: 32697992
DOI: 10.1016/j.celrep.2020.107930
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

건을2024-10-30부터공개중

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