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Showing 1–11 of 11 results
Advanced filters: Author: Amanda Kovach Clear advanced filters

  • The yeast Pmt4 is a membrane embedded protein Omannosyltransferase. Du et al found that Pmt4 assembles a homodimer and detects the coincidence of the S/T acceptor site and an adjacent S/T-X-S/T motif in a model substrate, ensuring modification only to the S/T-rich regions of acceptor substrates.

    • Minge Du
    • Zuanning Yuan
    • Huilin Li
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12

  • O-Mannosylation is an essential protein modification implicated in several diseases. Cryo-EM structures of the yeast mannosyltransferase complex Pmt1–Pmt2 bound to substrates reveal the substrate recognition model and confirm the reaction mechanism.

    • Lin Bai
    • Amanda Kovach
    • Huilin Li
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 704-711

  • PPARγ is a nuclear receptor that regulates metabolic homeostasis. It is activated by nitrated and oxidized fatty acids. The crystal structure of the ligand binding domain of PPARγ in complex with a physiological ligand, nitrated linoleic acid, is now described, showing differences with synthetic agonists that may have physiological relevance.

    • Yong Li
    • Jifeng Zhang
    • H Eric Xu
    Research
    Nature Structural & Molecular Biology
    Volume: 15, P: 865-867

  • The heterodimeric eukaryotic Drs2p-Cdc50p complex is a lipid flippase that maintains cell membrane asymmetry and its autoinhibition is released by PI4P binding. Here authors show cryo-EM structures of Drs2p-Cdc50p in apo and PI4P-activated form which reveal the structural changes upon PI4P binding.

    • Lin Bai
    • Amanda Kovach
    • Huilin Li
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • The high-resolution structure of the entire eukaryotic oligosaccharyltransferase complex is determined, revealing the role of membrane lipids in mediating inter-subunit interactions, and the mechanism by which the complex enables protein N-glycosylation.

    • Lin Bai
    • Tong Wang
    • Huilin Li
    Research
    Nature
    Volume: 555, P: 328-333

  • The fourteen members of the PYR/PYL family are receptors for the plant hormone abscisic acid (ABA). Now structural and functional work using the synthetic ligand pyrabactin, which inhibits seed germination, reveal that the PYL/PYR receptors respond differently to pyrabactin, elucidate the mechanisms for selective activation or inhibition of ABA receptors and allow the design of novel agonists.

    • Karsten Melcher
    • Yong Xu
    • H Eric Xu
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1102-1108

  • The plant hormone abscisic acid (ABA) is a regulator of plant growth, development and responses to environmental stresses. Recently, the PYR/PYL/RCAR family of START proteins was found to bind ABA and mediate inactivation of downstream effectors. The crystal structures of apo and ABA-bound receptors as well as a ternary PYL2–ABA–PP2C complex is now reported and analysed, revealing a gate–latch–lock mechanism underlying ABA signalling.

    • Karsten Melcher
    • Ley-Moy Ng
    • H. Eric Xu
    Research
    Nature
    Volume: 462, P: 602-608