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 2.80&Aring;" /> '''Structural Genomics ...)
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Revision as of 00:56, 21 November 2007

Image:1t7s.gif

1t7s, resolution 2.80Å

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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

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