ATP-dependent protein folding chaperone

Definition

Target type: molecularfunction

Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. [PMID:27365453]

ATP-dependent protein folding chaperones are molecular machines that assist in the proper folding of proteins. They are essential for maintaining cellular homeostasis, as misfolded proteins can lead to a variety of diseases. These chaperones bind to unfolded or partially folded proteins, preventing aggregation and promoting proper folding. This process is often driven by ATP hydrolysis, which provides the energy required for the chaperone to interact with the substrate protein and facilitate its folding. There are several types of ATP-dependent chaperones, each with its own specific function. Some, like Hsp70, act as "holding chaperones", binding to unfolded proteins and preventing aggregation. Others, like chaperonins, form large, barrel-shaped complexes that provide a protected environment for protein folding. Still others, like the proteasome, degrade misfolded proteins that cannot be rescued by chaperones. The activity of ATP-dependent protein folding chaperones is regulated by a variety of factors, including cellular stress, temperature, and the presence of unfolded proteins. This regulation ensures that chaperones are available when needed to prevent protein misfolding and aggregation.'
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Proteins (15)

Compounds (352)