Structural modeling of protein-RNA complexes using crosslinking of segmentally isotope-labeled RNA and MS/MS.
basic_science · Level V
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- Record sourced from PubMed, PMID 28346450.
- Also identified by DOI 10.1038/nmeth.4235 and PMC identifier 5505470.
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Abstract
Ribonucleoproteins (RNPs) are key regulators of cellular function. We established an efficient approach, crosslinking of segmentally isotope-labeled RNA and tandem mass spectrometry (CLIR-MS/MS), to localize protein-RNA interactions simultaneously at amino acid and nucleotide resolution. The approach was tested on polypyrimidine tract binding protein 1 and U1 small nuclear RNP. Our method provides distance restraints to support integrative atomic-scale structural modeling and to gain mechanistic insights into RNP-regulated processes.
Medical subject headings
- Heterogeneous-Nuclear Ribonucleoproteins
- Models, Molecular
- Nucleic Acid Conformation
- Polypyrimidine Tract-Binding Protein
- RNA
- Ribonucleoprotein, U1 Small Nuclear