TWGFD

Welcome to HSP70s !

The 70-kDa heat shock proteins (HSP70) are the most conserved group of HSP molecular chaperons, which are composed of two major domains (45-kDa N-terminal ATPase and 25-kDa peptide-binding domains) and two sub-domains (15-kDa β-sandwich and a C-terminal a-helical sub-domains). A peptide binding cleft which is responsible for interaction with the hydrophobic peptide fragment of unfolded proteins in an ATP controlled fashion is found in β-sandwich sub-domain of HSP70 proteins. The unique C-terminal region is composed of cytosol-specific conserved EEVD motif suggesting that the possible location of HSP70 is cytoplasm of the plant cell. Hsp70 constitute a highly conserved protein family of cellular chaperones widely distributed in plants, where they play a fundamental role in response to biotic and abiotic stress.