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Protein & Peptide Letters

Author(s): Danieli C. Goncalves, Lisandra M. Gava and Carlos H.I. Ramos

DOI: 10.2174/092986610790963708

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Human Hsp70/Hsp90 Organizing Protein (Hop) D456G Is a Mixture of Monomeric and Dimeric Species

Page: [492 - 498] Pages: 7

  • * (Excluding Mailing and Handling)

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.

Keywords: Heat shock protein, Hop, TPR domain, Protein folding, protein-protein interaction, Hsp90