人类热休克蛋白70/热休克蛋白90组织蛋白（Hop）D456G是单体和二聚体的混合物。

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

作者信息

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

机构信息

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

出版信息

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

DOI:10.2174/092986610790963708

PMID:19961430

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.

摘要

Hop是一种含有四肽重复结构域（TPR）的共伴侣蛋白，能够直接与Hsp70和Hsp90结合。先前的数据表明，TPR2A结构域是二聚化的主要位点，并且TPR2B结构域可能也在二聚化中发挥作用。我们展示了Hop-D456G，这是一种TPR2B结构域内的突变体，它是单体和二聚体的混合物。