1t7s | pdb_00001t7s
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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 Wed Nov 21 03:03:23 2007
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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 genomics
- Structural genomics
