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Volume 12 Issue 7, July 2005

Conus snails produce conotoxins that act on a variety of ion channels and receptors, including nicotinic acetylcholine receptors (nAChRs). The structure of a α-conotoxin variant bound to Aplysia acetylcholine binding protein reveals the likely mode of toxin interaction with nAChRs. Conus shell photos taken by K.S. Matz, courtesy of B. Olivera. pp 582-588

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  • The exosome is a complex composed of 3′→5′ exoribonucleases involved in RNA processing and degradation. The first high-resolution structure of the exosome core reveals a doughnut-like arrangement of six RNase PH–type subunits.

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  • The crystal structure of a four-protein complex comprising a SUMO ligase (E3), a SUMOylated protein substrate, and the cognate SUMO-conjugating enzyme sheds new light on catalysis, specificity and SUMO-protein interactions.

    • Michael J Matunis
    • Cecile M Pickart
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  • Four recent studies on the molecular architecture of amyloid fibrils made from different prion protein segments suggest commonalities among these fibrils. These studies also shed light on the structural distinctions between prion strains and the mechanism of fiber formation.

    • Susan W Liebman
    News & Views
  • MicroRNAs have established roles in negatively regulating messenger RNAs. Two plant microRNAs have recently been shown to target certain non-protein-coding RNAs for cleavage, adding a new dimension to the known roles of these tiny riboregulators.

    • Bonnie Bartel
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  • When and how the spliceosome assembles on its substrates in living yeast cells has been unclear. It is now evident that the 'when' is during transcription; the 'how' remains debatable.

    • Timothy W Nilsen
    News & Views
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