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=''> | ||
| - | Anything in this section will appear adjacent to the 3D structure and will be scrollable. | ||
| - | + | 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/Htpg2/1'> | + | |
| + | <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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| + | </StructureSection> | ||
| + | <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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