2bol: Difference between revisions
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Revision as of 10:58, 30 October 2007
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CRYSTAL STRUCTURE AND ASSEMBLY OF TSP36, A METAZOAN SMALL HEAT SHOCK PROTEIN
OverviewOverview
Small heat shock proteins (sHsps) are oligomers that perform a protective, function by binding denatured proteins. Although ubiquitous, they are of, variable sequence except for a C-terminal approximately 90-residue, "alpha-crystallin domain". Unlike larger stress response chaperones, sHsps, are ATP-independent and generally form polydisperse assemblies. One, proposed mechanism of action involves these assemblies breaking into, smaller subunits in response to stress, before binding unfolding substrate, and reforming into larger complexes. Two previously solved non-metazoan, sHsp multimers are built from dimers formed by domain swapping between the, alpha-crystallin domains, adding to evidence that the smaller subunits are, dimers. Here, the 2.5A resolution structure of an sHsp from the ... [(full description)]
About this StructureAbout this Structure
2BOL is a [Single protein] structure of sequence from [Taenia saginata] with SO4 as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Wrapping the alpha-crystallin domain fold in a chaperone assembly., Stamler R, Kappe G, Boelens W, Slingsby C, J Mol Biol. 2005 Oct 14;353(1):68-79. PMID:16165157
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