Key Residues Involved in Hsp70 Regulatory Activity and Affect of Co-Chaperones on Mechanism of Action

Title: Key Residues Involved in Hsp70 Regulatory Activity and Affect of Co-Chaperones on Mechanism of Action

Volume: 13 Issue: 7

Author(s): Yusuf Tutar

Affiliation:

Keywords: Stability, Hsp70, Ydj1

Abstract: Hsp70 proteins assist refolding of polypeptides in an ATP dependent manner. Crystal structure of intact Hsp70 protein has not been determined yet however, structures of its two domains were solved separately. Allostery between ATPase domain and peptide-binding domain facilitates unfolded substrate processing. To elucidate function of key residues and affect of other factors involved in this allosteric mechanism, a biochemical study was undertaken.

Cite this article as:

Tutar Yusuf, Key Residues Involved in Hsp70 Regulatory Activity and Affect of Co-Chaperones on Mechanism of Action, Protein & Peptide Letters 2006; 13 (7) . https://dx.doi.org/10.2174/092986606777790601