   7.4.2.3 | study of the structural interactions of Hsc70 ATPase domains with four different NEFs (nucleotide exchange factors) using PDB-ID: 1HPM. Two classes of key residues are distinguished in the domain: highly conserved residues involved in the nucleotide binding and not conserved but co-evolved and highly mobile residues, engaged in specific interactions with NEFs, i.e. N57, R258, R262, E283, And D285. Functional variability accompanied by structural variability at the co-chaperone binding sites and conservation/robustness both in terms of sequence and structural dynamics at the nucleotide binding sites are evolutionary optimized and is essential for adapting to interactions with differnent cofactors while meintaining ATPase activity |
