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Showing 1–11 of 11 results
Advanced filters: Author: Steven Stayrook Clear advanced filters

  • Sevenless, the Drosophila homologue of ROS1 (dROS1) is a receptor tyrosine kinase essential for the differentiation of photoreceptor cells and activated by binding to the GPCR Bride Of Sevenless (BOSS). Here, the authors use cryo-EM and HDX-MS to elucidate the structural details of dROS1 interaction with BOSS.

    • Jianan Zhang
    • Yuko Tsutsui
    • Daryl E. Klein
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12

  • De novo development of a simplified photosynthetic reaction center protein can clarify practical engineering principles needed to build enzymes for efficient energy conversion. Here, the authors develop an artificial photosynthetic reaction center that functions without the need for sacrificial electron donors or acceptors.

    • Nathan M. Ennist
    • Zhenyu Zhao
    • Christopher C. Moser
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10

  • Although small molecule tyrosine kinase inhibitors are effective in lung cancer driven by mutated EGFR, some receptor variants fail to respond. Here, the authors identify structural features of an important set of EGFR variants with reduced inhibitor sensitivity, guiding future inhibitor selection.

    • Iris K. van Alderwerelt van Rosenburgh
    • David M. Lu
    • Yuko Tsutsui
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-16

  • A vital component of influenza A virus' replication machinery is the M2 proton channel. Until recently, M2 was effectively targeted by amantadane-based antivirals, but resistance to these drugs is now so widespread that they have become ineffective. In the second of two related manuscripts, the crystal structure of a 25-residue fragment of M2, both with and without amantadine, is described. It is concluded that a single amantadine molecule binds in the centre of the M2 tetramer to physically occlude the pore.

    • Amanda L. Stouffer
    • Rudresh Acharya
    • William F. DeGrado
    Research
    Nature
    Volume: 451, P: 596-599

  • Drosophila Argos is an antagonist of EGF receptor signalling that functions by binding and sequestering EGFR ligands. The structure of Argos bound to the EGFR ligand Spitz reveals that Argos engulfs the ligand using three related domains with structural resemblance to receptors for TGF-β and urokinase plasminogen activator.

    • Daryl E. Klein
    • Steven E. Stayrook
    • Mark A. Lemmon
    Research
    Nature
    Volume: 453, P: 1271-1275