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6GBM

Solution structure of FUS-RRM bound to stem-loop RNA

Summary for 6GBM
Entry DOI10.2210/pdb6gbm/pdb
NMR InformationBMRB: 34259
DescriptorRNA-binding protein FUS, RNA (5'-R(*GP*GP*CP*AP*GP*AP*UP*UP*AP*CP*AP*AP*UP*UP*CP*UP*AP*UP*UP*UP*GP*CP*C)-3') (2 entities in total)
Functional Keywordsrna, rna recognition motif, rrm, rna binding protein
Biological sourceHomo sapiens (Human)
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Total number of polymer chains2
Total formula weight18575.86
Authors
Loughlin, F.E.,Allain, F.H.-T. (deposition date: 2018-04-15, release date: 2019-02-20, Last modification date: 2024-05-15)
Primary citationLoughlin, F.E.,Lukavsky, P.J.,Kazeeva, T.,Reber, S.,Hock, E.M.,Colombo, M.,Von Schroetter, C.,Pauli, P.,Clery, A.,Muhlemann, O.,Polymenidou, M.,Ruepp, M.D.,Allain, F.H.
The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity.
Mol. Cell, 73:490-504.e6, 2019
Cited by
PubMed Abstract: Fused in sarcoma (FUS) is an RNA binding protein involved in regulating many aspects of RNA processing and linked to several neurodegenerative diseases. Transcriptomics studies indicate that FUS binds a large variety of RNA motifs, suggesting that FUS RNA binding might be quite complex. Here, we present solution structures of FUS zinc finger (ZnF) and RNA recognition motif (RRM) domains bound to RNA. These structures show a bipartite binding mode of FUS comprising of sequence-specific recognition of a NGGU motif via the ZnF and an unusual shape recognition of a stem-loop RNA via the RRM. In addition, sequence-independent interactions via the RGG repeats significantly increase binding affinity and promote destabilization of structured RNA conformation, enabling additional binding. We further show that disruption of the RRM and ZnF domains abolishes FUS function in splicing. Altogether, our results rationalize why deciphering the RNA binding mode of FUS has been so challenging.
PubMed: 30581145
DOI: 10.1016/j.molcel.2018.11.012
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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