Key residues involved in Hsp70 regulatory activity and affect of co-chaperones on mechanism of action

TUTAR Y.

Protein and Peptide Letters, cilt.13, sa.7, ss.693-698, 2006 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 13 Sayı: 7
  • Basım Tarihi: 2006
  • Doi Numarası: 10.2174/092986606777790601
  • Dergi Adı: Protein and Peptide Letters
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.693-698
  • Anahtar Kelimeler: Hsp70, Stability, Ydj1
  • Recep Tayyip Erdoğan Üniversitesi Adresli: Hayır

Özet

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. © 2006 Bentham Science Publishers Ltd.