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

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

Volume: 17 Issue: 4

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

Affiliation:

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

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.

Cite this article as:

Goncalves C. Danieli, Gava M. Lisandra and Ramos H.I. Carlos, Human Hsp70/Hsp90 Organizing Protein (Hop) D456G Is a Mixture of Monomeric and Dimeric Species, Protein & Peptide Letters 2010; 17 (4) . https://dx.doi.org/10.2174/092986610790963708