Hsp70 protein binding

Definition

Target type: molecularfunction

Binding to a Hsp70 protein, heat shock proteins around 70kDa in size. [ISBN:0198506732]

Hsp70 proteins are molecular chaperones that play a critical role in maintaining cellular proteostasis. They bind to unfolded or misfolded proteins, preventing their aggregation and promoting their proper folding. This binding process is highly dynamic and involves multiple steps, starting with the recognition of exposed hydrophobic patches on the substrate protein. Hsp70s bind to these regions through their N-terminal ATPase domain, which undergoes conformational changes upon ATP hydrolysis. These changes allow for the recruitment of Hsp40 proteins, which act as substrate-binding partners for Hsp70, enhancing its binding affinity and specificity. Once bound, Hsp70 can either facilitate correct folding of the substrate protein, aided by other chaperones, or target it for degradation through the ubiquitin-proteasome system. The molecular function of Hsp70 protein binding, therefore, encompasses a range of activities including substrate recognition, ATP-dependent binding, substrate unfolding and refolding, and targeting for degradation. These functions are crucial for maintaining protein homeostasis, protecting cells from stress, and ensuring proper protein function.'
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Proteins (12)

Compounds (1,174)