Human Hsp70/Hsp90 organizing protein (Hop) D456G is a mixture of monomeric and dimeric species.
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.
Gonçalves
Danieli C
DC
Institute of Chemistry, University of Campinas-UNICAMP. P.O. Box 6154, 13083-970, Campinas, SP, Brazil.
Gava
Lisandra M
LM
Ramos
Carlos H I
CH
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002942:Circular Dichroism; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D016014:Linear Models; D008969:Molecular Sequence Data; D009154:Mutation; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
D006360:Heat-Shock Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; C079373:STIP1 protein, human