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Volume 10 Issue 8, August 2003

The crystal structure of the ear domain of GGA1 (red ribbon) in complex with a peptide (space-filling model, top) derived from p56. GGA1 is a monomeric adaptor protein for clathrin-coated vesicles; p56 is one of GGA1's protein ligand. This and the structure from a related study of the GGA3 ear domain reveal that conserved charged residues (purple space-filling model) on the GGA ear domains mediate the recognition of the hydrophobic phenylalanine in the peptides. Cover structure courtesy of B.M. Collins. See pages 599–606 and 607–613, News and Views pages 580–582.

Editorial

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News & Views

  • Two new structural studies reveal the nature of accessory protein binding to trans-Golgi network–specific adaptors of clathrin-coated vesicles.

    • Christine Knuehl
    • Frances M Brodsky
    News & Views
  • Structural and functional analysis of WASP family cell signaling proteins shows that the same residues that are sequestered upon GTPase binding in the autoinhibited state are involved in binding to and activating Arp2/3 complex, WASP's downstream partner in the signaling cascade.

    • Sarah E Hitchcock-DeGregori
    News & Views
  • IgA triggers immune responses by binding to Fc receptors on cells of the immune system. The structure of IgA1-Fc in a complex with two molecules of FcαRI provides clues that may explain the selectivity of IgA-mediated immune events.

    • Beth A Wurzburg
    • Theodore S Jardetzky
    News & Views
  • The structure of the calcium-bound core of human cardiac troponin reveals distinct subdomains connected by flexible linkers, implying that domain reorientation motions within the complex trigger muscle contraction.

    • Brian D Sykes
    News & Views
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