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Scientists solve structure of gene regulator that plays key role in cancer
Date:2/13/2008

stallize it.

Studies of the structure show that p300/CBP contains a binding pocket that is suitable for associating with a wide range of substrates the molecules it binds with and makes p300/CBP more promiscuous than other HATs, Marmorstein says.

In addition, p300/CBP uses a novel hit-and-run chemical mechanism to convert its substrates to the resulting protein products. The chemical mechanism differs from those employed by other HATs in that the histone substrate binds only transiently, leaving after a very brief encounter.

This hit-and-run mechanism is consistent with the enzymes ability to acetylate a variety of substrates because they dont have to bind in a very stable fashion, Marmorstein says.

The chemical mechanism employed by p300/CBP also bodes well for designing cancer drugs capable of pinpointing p300/CBP without affecting other enzymes and causing unwanted side effects. Because of p300/CBPs chemical mechanism, which differs from that of other HATs, an inhibitor that works against this family of enzymes likely wont work against the other ones, Marmorstein explains.

The scientists are now working to further elucidate the functions of p300/CBP and to solve larger structures of the protein. They plan to use the information they have already gained to develop inhibitors of p300/CBP activity research that will pave the way for the development of new anti-cancer therapies, Marmorstein says.


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Contact: Abbey Porter
aporter@wistar.org
215-898-3943
The Wistar Institute
Source:Eurekalert

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