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

Yusuf      Tutar

doi:10.2174/092986606777790601

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.

Keywords: Stability, Hsp70, Ydj1

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Protein & Peptide Letters

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

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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.

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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