1t7s
From Proteopedia
Structural Genomics of Caenorhabditis elegans: Structure of BAG-1 protein
Overview
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 beta-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.
About this Structure
1T7S is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Structural genomics of Caenorhabditis elegans: structure of the BAG domain., Symersky J, Zhang Y, Schormann N, Li S, Bunzel R, Pruett P, Luan CH, Luo M, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1606-10. Epub 2004, Aug 26. PMID:15333932 Page seeded by OCA on Sat May 3 09:38:32 2008
Categories: Caenorhabditis elegans | Single protein | Bunzel, R. | Li, S. | Luan, C H. | Luo, M. | Pruett, P. | SECSG, Southeast Collaboratory for Structural Genomics. | Schormann, N. | Symersky, J. | Zhang, Y. | Bag-1 cochaperone | Protein structure initiative | Psi | Secsg | Southeast collaboratory for structural genomic | Structural genomic
