Vol.45,No.7,2018
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Cover Story:The heat shock protein 90 (Hsp90) plays an important role in growth and progression of tumor cells through the appropriate folding, conformational maturation and activation of several hundred protein substrates (client proteins). Thus, Hsp90 attracts a great many of interests as a promising target for antitumor drugs which results in more than 20 inhibitors advancing to clinical trials. Here, we designed and synthesized a small molecule inhibitor: FS36 and the X-ray diffraction data of the complex crystal of Hsp90N-FS36 is collected. High-resolution X-ray crystallography shows that FS36 interacts with Hsp90N at the ATP-binding pocket and this demonstrates that FS36 possibly substitutes nucleotides to bind to Hsp90N. The complex crystal structure and the interactions between FS36 and Hsp90N lay the foundation of the design and majorization of novel antitumor drugs.
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Reviews and Monographs
Research Papers
Techniques and Methods
New techniques
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