CRYSTALLOGRAPHIC STUDIES OF HUMAN TOPOISOMERASE I DNA COMPLEX

$143,176P41FY2002RRNIH

Stanford University, Stanford CA

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Abstract

Human topoisomerase I is a 92 kDa enzyme that helps to control the level of DNA supercoiling 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 played a critical role in the structure determination of this important protein-DNA complex.

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