STRUCTURAL SIMILARITIES BETWEEN CHAPERONE MOLECULES OF THE HSP60 AND HSP70 FAMILIES DEDUCED FROM HYDROPHOBIC CLUSTER-ANALYSIS

In this study, the conservation of strong structural landmarks between all the members of two chaperone families (HSP60 and HSP70) was deduc ed from their sequences by hydrophobic cluster analysis. On this basis , we propose that the ATP-binding environment is maintained by a simil ar fold in both protein families. The observed similarities extend thr oughout the proteins, including both the ATPase domain and the C-termi nal substrate-binding domain.