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Volume 4 Issue 5, May 1997

Editorial

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News & Views

  • A convergence of technical advances in electron cryomicroscopy will allow visualization of biomolecular assemblies, without crystals, at resolutions below 10 Å. Recent cryomicroscopic structures of papillomavirus and hepatitis B virus capsid provide case studies.

    • Wah Chiu
    • Michael F. Schmid
    News & Views
  • The crystal structure of the yeast 20S proteasome not only provides further detail of the maws of this family of protein shredders, but also, has profound implications for the mechanism of peptide processing for antigen presentation.

    • James A. Brannigan
    • Guy G. Dodson
    News & Views
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Picture Story

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News & Views

  • Two complementary studies using fluorescence energy transfer with two different serpin–enzyme pairs provide the first glimpse of a stable serpin–proteinase complex.

    • Daniel A. Lawrence
    News & Views
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Progress

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Correspondence

  • The specific binding of N7-methylguanine cap analogues to the RNA methyltransferase VP39 was observed through X-ray crystallography, providing a prototypical structure for a complex between a protein and an mRNA 5′ cap.

    • Alec E. Hodel
    • Paul D. Gershon
    • Florante A. Quiocho
    Correspondence
  • Analysis of native serpin–protease complexes indicate that inhibition by serpins involves reactive centre cleavage and partial loop insertion, whereby the covalently linked protease migrates from the position of the initial attack to a position on the surface of the inhibitor β-sheet A to form a virtually irreversible complex.

    • Malgorzata Wilczynska
    • Ming Fa
    • Tor Ny
    Correspondence
  • Based on structures of five mutants of green fluorescent protein (GFP), we describe two conformational variants with differing charge distribution that explain the published absorption and fluorescence spectra of GFP mutants.

    • Gottfried J. Palm
    • Alexander Zdanov
    • Alexander Wlodawer
    Correspondence
  • Cofilin, a ubiquitous 15,000 Mr protein, plays a central role in regulating cytoskeletal dynamics. Cofilin binds to act in monomers and filaments, and has a pH-dependent actin severing activity. The structure will allow for a detailed analysis of cof ilin function.

    • A.A. Fedorov
    • P. Lappalainen
    • S.C. Almo
    Correspondence
  • Actophorin is a member of the actin-depolymerizing factor/cofilin family. It severs act in filaments and sequesters actin monomers. The crystal structure of actophorin will help to elucidate actin–ADF/cofilin interactions.

    • Shonda A. Leonard
    • Apostolos G. Gittis
    • Eaton E. Lattman
    Correspondence
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