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Showing 1–4 of 4 results
Advanced filters: Author: Małgorzata K. Dobaczewska Clear advanced filters

  • This study presents the crystal structure of a Fas-FADD complex, a central feature of the so-called death inducing signalling complex. The structure reveals a new mode of death domain interactions that allows four FADD and four Fas proteins in one complex.

    • Fiona L. Scott
    • Boguslaw Stec
    • Stefan J. Riedl
    Research
    Nature
    Volume: 457, P: 1019-1022

  • NSP and Cas family proteins form multidomain signaling platforms that integrate signals to mediate cell migration and invasion. Structural analyses show that the C-terminal domain of human NSP protein BCAR3 adopts the Cdc25-homology fold of Ras GTPase exchange factors, but in a closed conformation incompatible with enzymatic activity. Instead, this closed conformation is instrumental for interactions with Cas proteins.

    • Peter D Mace
    • Yann Wallez
    • Stefan J Riedl
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1381-1387

  • The first structure of fully active HOIP of the RBR family of RING-type E3 ligases in its transfer complex with an E2~ubiquitin conjugate provides insights into its mechanism of action, including the ideal alignment of the E2 and E3 catalytic centres for ubiquitin transfer and the allosteric regulation of the RBR family.

    • Bernhard C. Lechtenberg
    • Akhil Rajput
    • Stefan J. Riedl
    Research
    Nature
    Volume: 529, P: 546-550