Sandbox FEBS Gdansk 06
From Proteopedia
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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 | 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'>TextToBeDisplayed</scene> | <scene name='55/553925/Htpg1/2'>TextToBeDisplayed</scene> | ||
<scene name='55/553925/Htpg2/1'>TextToBeDisplayed</scene> | <scene name='55/553925/Htpg2/1'>TextToBeDisplayed</scene> | ||
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| + | <Structure load='2IOQ' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
Revision as of 11:18, 13 July 2013
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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