Literature summary for 7.4.2.3 extracted from

Liu, Y.; Gierasch, L.M.; Bahar, I.
Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs (2010), PLoS Comput. Biol., 6, e1000931.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Bos taurus

Crystallization (Comment)

Organism

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

Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Synonyms

Synonyms	Comment	Organism
HSP70 ATPase	-	Bos taurus

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Release 2023.1 (January 2023)