The TPR2B domain of the Hsp70/Hsp90 organizing protein (Hop) may contribute towards its dimerization

Protein Pept Lett. 2009;16(4):402-7. doi: 10.2174/092986609787848162.

Abstract

The role of the TPR2B domain of Hop is as yet unknown. We have shown here by site directed mutagenesis and size exclusion chromatography for the first time that the TPR1 and TPR2B domains of Hop independently dimerized, and that the dimerization of TPR2B was not dependent on its predicted two-carboxylate clamp residues. Furthermore, our data indicated that the dimerization of Hop and its domains was not disrupted in the presence of Hsp70 and Hsp90 peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Dimerization
  • Heat-Shock Proteins / chemistry*
  • Molecular Sequence Data
  • Protein Multimerization*
  • Protein Structure, Tertiary
  • Proteins / isolation & purification
  • Sequence Alignment

Substances

  • Heat-Shock Proteins
  • Proteins
  • STIP1 protein, human