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

Publisher: Bentham Science Publishers

E-ISSN: 1875-5305|17|4|492-498

ISSN: 0929-8665

Source: Protein and Peptide Letters, Vol.17, Iss.4, 2010-05, pp. : 492-498

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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.

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