Research: HSP90 unravelled

26 April 2006

The complete molecular structure of HSP90, one of the most exciting new anticancer drug targets was revealed this month. The breakthrough shows exactly how the protein works in cells and, more importantly, how it can be stopped by anticancer drugs.

HSP90 is a protein found in all cells and is vital for helping other proteins fold into their correct shape. However, cancer cells are especially dependent on HSP90, which makes them highly susceptible to inhibition. So molecules that block this protein kill cancer cells but have little effect on normal cells, and could be used to develop targeted treatments for cancers such as prostate, breast, bowel, ovarian and kidney.

The research team at the Institute of Cancer Research, led by Professor Laurence Pearl, was funded by The Wellcome Trust and benefited from the infrastructure support at The Institute of Cancer Research from Cancer Research UK.

External links

• Laurence H. Pearl et al, Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
• The Institute of Cancer Research
• Cancer Research UK " target="_blank">Cancer Research UK

Image credit: Dr David Becker. The image from our Medical Photo Library shows two human breast cancer cells dividing. The cell at the top is at prophase, showing the condensing chromosomes prior to their separation. The cell at the bottom is in anaphase, where the chromosomes are in the process of pulling apart.