NMR assignment of the N-terminal region of human La free and in complex with RNA.
(1)H, (15)N and (13)C chemical shift assignments are presented for the N-terminal region of human La protein, in the apo and 5'-UUUU RNA-bound state. Secondary structure analysis shows conformational changes in the interdomain linker upon complex formation.
Sanfelice
Domenico
D
Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, UK.
Kelly
Geoff
G
Curry
Stephen
S
Conte
Maria R
MR
D000595:Amino Acid Sequence; D001324:Autoantigens / Q000737:chemistry*; D001665:Binding Sites; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011522:Protons; D012313:RNA / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry*
D001324:Autoantigens; D002247:Carbon Isotopes; C506261:SSB protein, human; D009587:Nitrogen Isotopes; D010446:Peptide Fragments; D011522:Protons; D016601:RNA-Binding Proteins; D012313:RNA