Two high-resolution structures of the human E3 ubiquitin ligase Siah1

V. Rimsa, T. C. Eadsforth, W. N. Hunter

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)

    Abstract

    Siah1 is an E3 ubiquitin ligase that contributes to proteasome-mediated degradation of multiple targets in key cellular processes and which shows promise as a therapeutic target in oncology. Structures of a truncated Siah1 bound to peptide-based inhibitors have been reported. Here, new crystallization conditions have allowed the determination of a construct encompassing dual zinc-finger subdomains and substrate-binding domains at significantly higher resolution. Although the crystals appear isomorphous, two structures present distinct states in which the spatial orientation of one zinc-finger subdomain differs with respect to the rest of the dimeric protein. Such a difference, which is indicative of conformational freedom, infers potential biological relevance related to recognition of binding partners. The crystallization conditions and improved models of Siah1 may aid future studies investigating Siah1-ligand complexes.
    Original languageEnglish
    Pages (from-to)1339-1343
    Number of pages5
    JournalActa Crystallographica F-Structural Biology and Crystallization Communications
    Volume69
    Issue number12
    DOIs
    Publication statusPublished - Dec 2013

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