Human topoisomerase I is a 92 kDa enzyme that helps to control the level of DNA supercoiling in cells. It is also found to be the sole target of camptothecin, an extremely promising anti-cancer drug currently in clinical trials. Elucidating the three-dimensional structure of topoisomerase I bound to DNA would allow us to unravel the fascinating mechanism of this enzyme, and would facilitate the design of improved anti-cancer drugs. We are currently well on our way to determining the crystal structure of human topoisomerase I bound to DNA. Synchrotron radiation has play a critical role in the structure determination of this important protein-DNA complex.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR001209-23S1
Application #
6658534
Study Section
Project Start
2002-03-01
Project End
2003-02-28
Budget Start
Budget End
Support Year
23
Fiscal Year
2002
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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