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2000
Volume 17, Issue 4
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Hop is a tetratricopeptide repeat domain (TPR)-containing co-chaperone that is able to directly associate with both Hsp70 and Hsp90. Previous data showed that the TPR2A-domain is the primary site for dimerization and that the TPR2B-domain may also play a role in dimerization. We present Hop-D456G, a mutant within the TPR2B-domain, that is a mixture of monomeric and dimeric species.

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/content/journals/ppl/10.2174/092986610790963708
2010-05-01
2025-06-28
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/content/journals/ppl/10.2174/092986610790963708
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  • Article Type:
    Research Article
Keyword(s): Heat shock protein; Hop; Hsp90; Protein folding; protein-protein interaction; TPR domain
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