• Molecular basis for arginine C-terminal degron recognition by Cul2 FEM1 E3 ligase

    15 days ago - By ACS Division of Biological Chemistry

    Nature Chemical Biology, Published online: 04 January 2021; doi:10.1038/s41589-020-00704-3 Structural characterization of the substrate adapters of the C-degron pathway reveals the selective recognition mode towards substrates with C-terminal arginine by FEM1A/C and FEM1B.
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  • Bottom-up de novo design of functional proteins with complex structural features

    15 days ago - By ACS Division of Biological Chemistry

    Nature Chemical Biology, Published online: 04 January 2021; doi:10.1038/s41589-020-00699-x Beginning with a functional site and building a supporting scaffold around it enables the de novo design of proteins with distinct binding motifs for use in biosensors to detect antibody responses and as ligands of synthetic signaling receptors.
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  • Molecular basis for ubiquitin ligase CRL2 FEM1C -mediated recognition of C-degron

    15 days ago - By ACS Division of Biological Chemistry

    Nature Chemical Biology, Published online: 04 January 2021; doi:10.1038/s41589-020-00703-4 Crystal structures of FEM1C in apo and in complex with a C-degron ending with arginine reveal a binding pocket in FEM1C that recognizes C-degrons and the essential role of C-terminal arginine for recognition.
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  • Conformational rearrangement during activation of a metabotropic glutamate receptor

    15 days ago - By ACS Division of Biological Chemistry

    Nature Chemical Biology, Published online: 04 January 2021; doi:10.1038/s41589-020-00702-5 Single-molecule FRET of mGluR2 shows that the conformations of the ligand-binding domain and the linked cysteine-rich domain are loosely coupled during ligand-induced activation and defines two pre-active states linking inactive and active states.
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