Hsp90 protein binding

Definition

Target type: molecularfunction

Binding to Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size. [GOC:ai]

Hsp90 is a molecular chaperone that plays a crucial role in the folding, stabilization, and trafficking of a wide range of client proteins involved in essential cellular processes. Hsp90 proteins bind to their client proteins through a complex and dynamic mechanism, utilizing a combination of hydrophobic interactions, hydrogen bonds, and electrostatic interactions. The binding process often involves a two-step mechanism, beginning with a low-affinity interaction followed by a conformational change in both Hsp90 and the client protein, leading to high-affinity binding. Hsp90 possesses a unique structure consisting of three domains: the N-terminal domain (NTD), the middle domain (MD), and the C-terminal domain (CTD). The NTD harbors the ATP-binding site and is responsible for ATP hydrolysis, a key step in the chaperone cycle. The MD contains a client-binding site and mediates interactions with co-chaperones. The CTD promotes dimerization, forming a symmetric dimer that is essential for function. In the context of Hsp90's molecular function, its client binding is crucial for maintaining cellular homeostasis and regulating a wide array of cellular processes. Hsp90's client proteins encompass a diverse set of proteins, including kinases, transcription factors, steroid hormone receptors, and other proteins involved in signal transduction, cell cycle control, and stress response. By binding to these client proteins, Hsp90 stabilizes their conformation, promotes their folding, and facilitates their interaction with other proteins, ultimately influencing their activity and function. Furthermore, Hsp90's chaperone activity extends to its interaction with co-chaperones. These co-chaperones, such as Hop, p23, and Aha1, contribute to the intricate regulatory network surrounding Hsp90, fine-tuning its chaperone activity and influencing its interactions with client proteins. The interplay between Hsp90, client proteins, and co-chaperones forms a dynamic system that is crucial for maintaining cellular function and responding to various cellular stresses. The disruption of Hsp90's chaperone activity, often due to genetic mutations or environmental factors, can lead to misfolding, aggregation, and dysfunction of client proteins, contributing to the development of various diseases.'
```"

Proteins (20)

Compounds (826)