Showing papers by "Toby J. Gibson published in 1995"
887 citations
TL;DR: The double‐stranded RNA binding domain (dsRBD) is a approximately 70 residue motif found in a variety of modular proteins exhibiting diverse functions, yet always in association with dsRNA, and the structure of the RNase III protein, an enzyme present in most, perhaps all, living cells, is reported here.
Abstract: The double-stranded RNA binding domain (dsRBD) is a approximately 70 residue motif found in a variety of modular proteins exhibiting diverse functions, yet always in association with dsRNA. We report here the structure of the dsRBD from RNase III, an enzyme present in most, perhaps all, living cells. It is involved in processing transcripts, such as rRNA precursors, by cleavage at short hairpin sequences. The RNase III protein consists of two modules, a approximately 150 residue N-terminal catalytic domain and a approximately 70 residue C-terminal recognition module, homologous with other dsRBDs. The structure of the dsRBD expressed in Escherichia coli has been investigated by homonuclear NMR techniques and solved with the aid of a novel calculation strategy. It was found to have an alpha-beta-beta-beta-alpha topology in which a three-stranded anti-parallel beta-sheet packs on one side against the two helices. Examination of 44 aligned dsRBD sequences reveals several conserved, positively charged residues. These residues map to the N-terminus of the second helix and a nearby loop, leading to a model for the possible contacts between the domain and dsRNA.
277 citations
TL;DR: This work reviews recent findings and presents new hypotheses into the structural and functional properties of the actin‐binding domain, central coiled‐coil region and regulatory/membrane protein‐binding regions of dystrophin and utrophin.
147 citations
TL;DR: In this paper, NMR spectroscopy was used to determine the secondary structure in solution of a KH domain (repeat 5 from vigilin) and almost complete assignments were obtained for the 1H and 15N resonances using uniform 15N-labeling of the protein combined with homo-nuclear 2D 1HNMR and 3D 15N correlated 1H NMR.
34 citations
01 Jan 1995
TL;DR: In this paper, NMR spectroscopy was used to determine the secondary structure in solution of a KH domain (repeat 5 from vigilin), almost complete assignments were obtained for the ~H and ~SN resonances using uniform ~SN-labeling of the protein combined with homo-nuclear 2D ~HNMR and 3D lSN correlated ~H NMR.
Abstract: The KH module has recently been identified in a num- ber of RNA associated proteins including vigilin and FMR1, a protein implicated in the fragile X syndrome. In this work, NMR spectroscopy was used to determine the secondary structure in solution of a KH domain (repeat 5 from vigilin). Almost complete assignments were obtained for the ~H and ~SN resonances using uniform ~SN-labeling of the protein combined with homo-nuclear 2D ~HNMR and 3D lSN correlated ~H NMR. On the basis of NOE patterns, secondary chemical shifts and amide solvent expo- sure, the secondary structure consists of an antiparallel three stranded fl sheet connected by two helical regions. This domain may also be stabilized by an appended C-terminal helix which is common to many but not all members of the KH family.
33 citations