Human Hsp70/Hsp90 organizing protein (Hop) D456G is a mixture of monomeric and dimeric species

Danieli C Gonçalves; Lisandra M Gava; Carlos H I Ramos

doi:10.2174/092986610790963708

Human Hsp70/Hsp90 organizing protein (Hop) D456G is a mixture of monomeric and dimeric species

Protein Pept Lett. 2010 Apr;17(4):492-8. doi: 10.2174/092986610790963708.

Authors

Danieli C Gonçalves¹, Lisandra M Gava, Carlos H I Ramos

Affiliation

¹ Institute of Chemistry, University of Campinas-UNICAMP. P.O. Box 6154, 13083-970, Campinas, SP, Brazil.

PMID: 19961430
DOI: 10.2174/092986610790963708

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Chromatography, Gel
Circular Dichroism
Dimerization
Escherichia coli / genetics
Escherichia coli / metabolism
Heat-Shock Proteins / chemistry*
Heat-Shock Proteins / genetics
Heat-Shock Proteins / metabolism
Humans
Linear Models
Molecular Sequence Data
Mutation
Protein Subunits
Recombinant Proteins / biosynthesis
Recombinant Proteins / chemistry
Recombinant Proteins / genetics

Substances

Heat-Shock Proteins
Protein Subunits
Recombinant Proteins
STIP1 protein, human