Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis.
The main limitation in NMR-determined structures of nucleic acids and their complexes with proteins derives from the elongated, non-globular nature of physiologically important DNA and RNA molecules. Since it is generally not possible to obtain long-range distance constraints between distinct regions of the structure, long-range properties such as bending or kinking at sites of protein recognition cannot be determined accurately nor precisely. Here we show that use of residual dipolar couplings in the refinement of the structure of a protein-RNA complex improves the definition of the long-range properties of the RNA. These features are often an important aspect of molecular recognition and biological function; therefore, their improved definition is of significant value in RNA structural biology.
Bayer
P
P
MRC Laboratory of Molecular Biology, Cambridge, U.K.
Varani
L
L
Varani
G
G
D003001:Cloning, Molecular; D004134:Dimyristoylphosphatidylcholine; D004926:Escherichia coli; D006801:Humans; D008051:Lipid Bilayers; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010742:Phospholipid Ethers; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
C052298:1,2-dihexadecyl-sn-glycero-3-phosphocholine; D008051:Lipid Bilayers; D010742:Phospholipid Ethers; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear; C075339:U1A protein; D012313:RNA; D004134:Dimyristoylphosphatidylcholine