The E3 Ubiquitin Ligase CHIP and the Molecular Chaperone Hsc70 Form a Dynamic, Tethered Complex

The E3 ubiquitin ligase CHIP (C-terminus of Hsc70 Interacting Protein, a 70 kDa homodimer) binds to the molecular chaperone Hsc70 (a 70 kDa monomer) and this complex is important in both the ubiquitination of Hsc70 and the turnover of Hsc70-bound clients. Here we used NMR spectroscopy, bio-layer int...

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Hlavní autoři: Smith, Matthew C., Scaglione, K. Matthew, Assimon, Victoria A., Patury, Srikanth, Thompson, Andrea D., Dickey, Chad A., Southworth, Daniel R., Paulson, Henry L., Gestwicki, Jason E., Zuiderweg, Erik R.P.
Médium: Artigo
Jazyk:Inglês
Vydáno: 2013
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Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3856692/
https://ncbi.nlm.nih.gov/pubmed/23865999
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi4009209
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