The key function of protein molecule Hsp90 is to stabilize the regulatory system which controls the cells of our body.
According to LAURENCE PEARL {prof. in structural biology in genome damage and stability at univ. of sussex UK } an insight into the nitty-gritty of the structure of this protein can lead to the development of a brand new drug that may be the answer to the cancer.
He also explains that Hsp 90 is a molecule "chaperone" that stabilizes & help activate client proteins involved in many of the signalling and regulatory path ways in our cell, including some that are involved in cancer
Its also becoming clear that many viruses use the host cell Hsp90 to help assemble their protein and in some parasite the Hsp90 system is important for infection.
BIG QUESTION...
Pearl and his team are trying to understand how a particular client protein associate with the Hsp90 system, and what Hsp90 does to them that helps them to attain the active state.
Using biochemistry and structural techniques, he and his team has been able to determine the the atomic structure of Hsp90 and define a "motor" activity that is driven by the energy molecule of the cell, ATP
He has also been able to determine the structure of some of the "co-chaperones" that cooperate with Hsp90 and help regulate it and define how they do this.
The big question that still is to be answered is how Hsp90 and its co-chaperones interact with the client protein.
The studies will also allow us to define that why some proteins need Hsp90 and some don't and start to design highly specific inhibitors that prevent some client proteins from accessing the chaperone, while allowing the system as an whole to continue to operate.
According to LAURENCE PEARL {prof. in structural biology in genome damage and stability at univ. of sussex UK } an insight into the nitty-gritty of the structure of this protein can lead to the development of a brand new drug that may be the answer to the cancer.
He also explains that Hsp 90 is a molecule "chaperone" that stabilizes & help activate client proteins involved in many of the signalling and regulatory path ways in our cell, including some that are involved in cancer
Its also becoming clear that many viruses use the host cell Hsp90 to help assemble their protein and in some parasite the Hsp90 system is important for infection.
BIG QUESTION...
Pearl and his team are trying to understand how a particular client protein associate with the Hsp90 system, and what Hsp90 does to them that helps them to attain the active state.
Using biochemistry and structural techniques, he and his team has been able to determine the the atomic structure of Hsp90 and define a "motor" activity that is driven by the energy molecule of the cell, ATP
He has also been able to determine the structure of some of the "co-chaperones" that cooperate with Hsp90 and help regulate it and define how they do this.
The big question that still is to be answered is how Hsp90 and its co-chaperones interact with the client protein.
ROAD AHEAD...
The future focus of the project is to obtain the atomic structure for a particular class of client protein beyond the Hsp90 chaperone system.The studies will also allow us to define that why some proteins need Hsp90 and some don't and start to design highly specific inhibitors that prevent some client proteins from accessing the chaperone, while allowing the system as an whole to continue to operate.
No comments:
Post a Comment