Sandbox FEBS Gdansk 06
From Proteopedia
(Difference between revisions)
(New page: == Your Heading Here (maybe something like 'Structure') == <StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry 1dq8)' scene=''> Any...) |
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| - | + | == Structure of HtpG == | |
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| + | 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 | ||
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| + | <scene name='55/553925/Htpg1/2'>HtpG - evolutionary conservation</scene> | ||
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| + | <scene name='55/553925/Htpg2/1'>polar aa of HtpG</scene> | ||
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<Structure load='2IOQ' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='2IOQ' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
Current revision
Structure of HtpG
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>
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