Sandbox FEBS Gdansk 06
From Proteopedia
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== Structure of HtpG == | == Structure of HtpG == | ||
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''> | <StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''> | ||
| - | + | In eukaryotes, the ubiquitous and abundant members of the 90 kilodalton heat-shock protein (hsp90) chaperone family facilitate the folding and conformational changes of a broad array of proteins important in cell signaling, proliferation, and survival. Here we describe the effects of nucleotides on the structure of full-length HtpG, the Escherichia coli hsp90 ortholog | |
</StructureSection> | </StructureSection> | ||
Revision as of 11:15, 13 July 2013
Structure of HtpG
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