Structural genomics of Caenorhabditis elegans: Structure of the BAG domain

J. Symersky, Y. Zhang, N. Schormann, S. Li, R. Bunzel, P. Pruett, C. H. Luan, M. Luo*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    6 Scopus citations

    Abstract

    Binding of the BAG domain to the eukaryotic chaperone heat-shock protein (Hsp70) promotes ATP-dependent release of the protein substrate from Hsp70. Although the murine and human BAG domains have been shown to form an antiparallel three-helix bundle, the Caenorhabditis elegans BAG domain is formed by two antiparallel helices, while the third helix is extended away and stabilized by crystal-packing interactions. A small β-sheet between helices 2 and 3 interferes with formation of the intramolecular three-helix bundle. However, intermolecular three-helix bundles are observed throughout the crystal packing and suggest that stable functional dimers and tetramers can be formed in solution. The structure may represent a new folding type of the BAG domain.

    Original languageEnglish (US)
    Pages (from-to)1606-1610
    Number of pages5
    JournalActa Crystallographica Section D: Biological Crystallography
    Volume60
    Issue number9
    DOIs
    StatePublished - Sep 1 2004

    ASJC Scopus subject areas

    • Structural Biology

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