Carboxylate clamp tetratricopeptide repeat (TPR) domain containing Hsp90 cochaperones in Triticeace: An insight into structural and functional diversification

D Mishra, S Shekhar, S Chakraborty… - … and experimental botany, 2018 - Elsevier
The molecular chaperones serve as surveillance molecules that mediates regulatory
crosstalk between protein folding and degradation pathways under natural and stress
conditions. In present study, we focused on the diversification and role of tetratricopeptide
repeat (TPR) domain containing Hsp90 cochaperones. These cochaperone were
recognized by the presence of three motifs of TPR with the basic conserved residues often
referred to as carboxylate clamp (CC). A total of 213 putative CC-TPRs were found in …

Carboxylate clamp tetratricopeptide repeat (TPR) domain containing Hsp90 cochaperones in Triticeace: an insight into structural and functional diversification.

DM Divya Mishra, SS Shubhendu Shekhar… - 2018 - cabidigitallibrary.org
The molecular chaperones serve as surveillance molecules that mediates regulatory
crosstalk between protein folding and degradation pathways under natural and stress
conditions. In present study, we focused on the diversification and role of tetratricopeptide
repeat (TPR) domain containing Hsp90 cochaperones. These cochaperone were
recognized by the presence of three motifs of TPR with the basic conserved residues often
referred to as carboxylate clamp (CC). A total of 213 putative CC-TPRs were found in …
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