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1t7s
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(New page: 200px<br /><applet load="1t7s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t7s, resolution 2.80Å" /> '''Structural Genomics ...)
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Revision as of 00:56, 21 November 2007
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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
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 genomics | Structural genomics
