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18 Jul, 2011
By: Admission Jankari
The key function of the protein molecule, Hsp90, is to stabilise the regulatory systems which control the cells of our body. According to Laurence Pearl, who
heads the School of Life Sciences at the University of Sussex, UK, an insight into the nitty-gritty of the structure of this protein can lead to the development of new drugs, which may be the answer to cancer.
Pearl, also a professor of structural biology in the Genome Damage and Stability Centre at Sussex, explains that Hsp90 is a molecular ‘chaperone’
that stabilises and helps activate ‘client’ proteins involved in many of the main signalling and regulatory pathways in our cells, including some that are involved in cancer.
“It is also becoming clear that many viruses use the host cell Hsp90 to help assemble their proteins and in some parasites the Hsp90 system is important for infection,” he says.
> BIG QUESTIONS
Pearl and his team are trying to understand how particular client proteins associate with the Hsp90 system, and what Hsp90 does to them or for them that helps them attain their active state. Using biochemistry and structural techniques (such as X-ray crystallography and electron microscopy), Pearl and his team have been able to determine the atomic structure of Hsp90 and define a ‘motor’ activity that is driven by the energy molecule of the cell, ATP.
“We have also been able to determine the structure of some of the cochaperones that co-operate with Hsp90 and help regulate it and define how they do this. The big questions that still remain to be answered relate to how Hsp90 and its co-chaperones interact with the client proteins,” he says.
As to the challenges of such a project,
Pearl says, it can only be carried out if we can make all the different proteins we wish to study in sufficient quantity and at very high levels of purity. Once this is achieved, the main challenge, he adds, is in getting the proteins and their complexes to crystallise so that certain experiments can be done to determine the atomic structures.
The involvement of the Hsp90 system in many forms of cancer and in some viral and parasitic diseases has led to considerable interest in developing drugs that stop Hsp90 from working.
> ROAD AHEAD
As to the future agenda of the project, Pearl explains that the current focus is on obtaining atomic structures for a particular class of client proteins bound to the Hsp90 chaperone system.
“These studies will allow us to define why some proteins need Hsp90 and some don’t and to start to design highly specific inhibitors that prevent some clients from accessing the chaperone, while allowing the system as a whole to continue to operate,” he sums up.
The university and the team would require more qualified people to assist them in their research work. Hence, postgraduate students of life sciences and inter-related disciplines in India keen on research in such areas can apply to the university
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