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The C-terminal "BAG domain" of BAG-1 mediates the interaction with the Hsc70 and Hsp70 heat shock proteins [ 3], molecular chaperones that bind proteins in non-native states assisting them to reach a functional active conformation [ 4].
The core of the BAG domain comprises two anti-parallel alpha-helices that mediate interaction with the HSC70 and HSP70 heat shock proteins (Briknarova et al, 2001; Sondermann et al, 2001), molecular chaperones that bind proteins in non-native states assisting them to reach functional confirmations.
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HSPs in the normal cell state assist in the folding of native polypeptides, and their induction under stress conditions prevents production of cytotoxins and stabilises denatured proteins (e.g., [32], [58], [59]).
Molecular chaperones are a diverse family of proteins expressed by both prokaryotic and eukaryotic organisms that serve to maintain correct protein folding in a 3-dimensional functional state, assist in multiprotein complex assembly and protect proteins from irreversible aggregation at synthesis and during conditions of cellular stress [ 267].
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