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Chaperone protein ClpB
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | + | The 3D structure of ClpB complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: N-terminal, nucleotide-binding domain (NBD) 1, a long coiled-coil linker domain, a second NBD and a D2 small domain. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 09:15, 4 July 2022
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References
- ↑ 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
- ↑ Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell. 2003 Oct 17;115(2):229-40. PMID:14567920
