Combining NMR Spectroscopy and Molecular Dynamic Simulations to Solve and Analyze the Structure of Protein-RNA Complexes
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
30611432
DOI
10.1016/bs.mie.2018.09.002
PII: S0076-6879(18)30359-8
Knihovny.cz E-resources
- Keywords
- MD simulation, Protein–RNA interactions, Solution-state NMR, Structures,
- MeSH
- CELF Proteins chemistry metabolism MeSH
- Protein Interaction Domains and Motifs MeSH
- Nucleic Acid Conformation MeSH
- Protein Conformation, alpha-Helical MeSH
- Protein Conformation, beta-Strand MeSH
- Humans MeSH
- Magnetic Resonance Spectroscopy methods MeSH
- RNA chemistry genetics metabolism MeSH
- RNA Splicing Factors chemistry metabolism MeSH
- Molecular Dynamics Simulation * MeSH
- Thermodynamics MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Hydrogen Bonding MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- CELF Proteins MeSH
- RBFOX1 protein, human MeSH Browser
- RNA MeSH
- RNA Splicing Factors MeSH
Understanding the RNA binding specificity of protein is of primary interest to decipher their function in the cell. Here, we review the methodology used to solve the structures of protein-RNA complexes using solution-state NMR spectroscopy: from sample preparation to structure calculation procedures. We also describe how molecular dynamics simulations can help providing additional information on the role of key amino acid side chains and of water molecules in protein-RNA recognition.
References provided by Crossref.org
In Vitro Evolution Reveals Noncationic Protein-RNA Interaction Mediated by Metal Ions
MD simulations reveal the basis for dynamic assembly of Hfq-RNA complexes
