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

7 Scopus citations


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
Issue number9
StatePublished - Sep 2004

ASJC Scopus subject areas

  • Structural Biology


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