Ribonucleoprotein domain

Ribosomes are ancient ribonucleoprotein complexes that are the sites of protein synthesis in living cells. Their core structures and fundamental functional mechanisms have been conserved throughout the three domains of life bacteria, archaea and eukaryotes. All ribosomes are organized into two subunits that are defined by their apparent sedimentation coefficient, measured in Svedberg units (S). There is a general... 

Domain involved in protein-protein interaction, originally described in transcription factors LINl, ISLl, and MED3 Long interspersed nuclear element Liquid-liquid extraction Lower limit of detection Lower limit of quantification Large nuclear ribonucleoprotein Limit of detection logjo of odds... 

The La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3 poly(U)-rich elements of nascent RNA polymerase III (pol III) transcripts to assist folding and maturation. Alfano et al have determined the solution structure of N-terminal domain from La show that the La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices. Chemical shift mapping experiments show that these insertions are involved in RNA interactions ll... 

Lapinaite and colleagues have published a particularly impressive study of the box C/D ribonucleoprotein (RNP) from the archaeon Pyrococcus furiosus, a complex of 390 kDa responsible for methylating ribosomal RNA. ° By I, L, V-methyl labelling the three protein components of the complex, methyl TROSY spectra were used to monitor chemical shifts and PREs. Models for the entire complex could thus be calculated both with and without substrate RNA present using previously-determined structures of protein and RNA sub-units. Domain boundaries were allowed to be flexible during docking using NMR and SANS data, with... 

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