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Chaperone protein ClpB

From Proteopedia

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<StructureSection load='1qvr' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='1qvr' size='340' side='right' caption='Thermus thermophilus ClpB (PDD ID [[1qvr]])' scene=''>
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This is a default text for your page '''Chaperone protein ClpB'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
== Function ==
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'''Chaperone protein ClpB''' (ClpB) reactivates aggregated proteins in cooperation with Hsp70<ref>PMID:24843029</ref>. ClpB is an ATP-dependent chaperone which can rescue proteins from an aggregated state.
== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>

Revision as of 08:54, 4 July 2022

Thermus thermophilus ClpB (PDD ID 1qvr)

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References

  1. ↑ Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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