Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.

ABSTRACT: Heat-shock protein 90 (HSP90) is a highly active molecular chaperone that plays a crucial role in cellular function. It facilitates the folding, assembly and stability of various oncogenic proteins, particularly kinases and transcription factors involved in regulating tumor growth and maintenance signaling pathways. Consequently, HSP90 inhibitors are being explored as drugs for cancer therapy. Crystallographic fragment screening is a novel screening method that has been developed in recent years for fragment-based drug discovery and is known for its high hit rate and its ability to provide direct insights into the complex structures of proteins and compounds. In this paper, high-diffraction-resolution crystals of the N-terminal domain of human HSP90α were employed in crystallographic fragm

SUBMITTER: Huang L 

PROVIDER: S-EPMC11878448 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature