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Article

Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF.

Nature - 13 Jul 2011

Mackereth Cameron D, Madl Tobias, Bonnal Sophie, Simon Bernd, Zanier Katia, Gasch Alexander, Rybin Vladimir, Valcárcel Juan, Sattler Michael

Abstract excerpt

Many cellular functions involve multi-domain proteins, which are composed of structurally independent modules connected by flexible linkers. Although it is often well understood how a given domain recognizes a cognate oligonucleotide or peptide motif, the dynamic interaction of multiple domains in the recognition of these ligands remains to be characterized. Here we have studied the molecular mechanisms of the...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 21753750
DOI: 10.1038/nature10171

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF.PMID 21753750Read ↗

Recognition of the 3' splice site RNA by the U2AF heterodimer involves a dynamic population shift.Semantic proximity Read ↗

Structure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA.Semantic proximity Read ↗

Pre-mRNA Splicing Factor U2AF2 Recognizes Distinct Conformations of Nucleotide Variants at the Center of the pre-mRNA Splice Site SignalSemantic proximity Read ↗

A novel function for the U2AF 65 splicing factor in promoting pre-mRNA 3'-end processing.Semantic proximity Read ↗

All-Atom Simulations Elucidate the Impact of U2AF2 Cancer-Associated Mutations on Pre-mRNA Recognition.Semantic proximity Read ↗

Mechanisms for U2AF to define 3' splice sites and regulate alternative splicing in the human genome.Semantic proximity Read ↗

Promiscuity in protein-RNA interactions: conformational ensembles facilitate molecular recognition in the spliceosome: conformational diversity in U2AF⁶⁵ facilitates binding to diverse RNA sequences.Semantic proximity Read ↗

A splice site-sensing conformational switch in U2AF2 is modulated by U2AF1 and its recurrent myelodysplasia-associated mutation.Semantic proximity Read ↗

The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF 65) is essential in vivo but dispensable for activity in vitro.Semantic proximity Read ↗

Structures of SF3b1 reveal a dynamic Achilles heel of spliceosome assembly: Implications for cancer-associated abnormalities and drug discovery.Semantic proximity Read ↗

Cancer-Related Mutations Alter RNA-Driven Functional Cross-Talk Underlying Premature-Messenger RNA Recognition by Splicing Factor SF3b.Semantic proximity Read ↗

A Splice Site-Sensing Conformational Switch in U2AF2 is Modulated by U2AF1 and its Recurrent Myelodysplasia-Associated MutationSemantic proximity Read ↗

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