Journal
ANTI-CANCER AGENTS IN MEDICINAL CHEMISTRY
Volume 9, Issue 1, Pages 51-54Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/187152009787047716
Keywords
Sumoylation; Ubc9; virtual screen; structure
Categories
Funding
- NIH Center of Biomedical Research Excellence in Molecular Targets [5P20 RR 018733]
- NIH [R01GM079516]
- James Graham Brown Cancer Center Lung Cancer Fellowship
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR018733] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM079516] Funding Source: NIH RePORTER
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Sumoylation has been implicated in a variety of cancers, suggesting that sumoylation manipulation could be one approach for regulating tumorgenesis. Ubc9 exerts a central function for the sumoylation pathway, interacting with almost all the partners required for sumoylation. The high-resolution structure available for Ubc9 as well as the recent determination of more interacting partner complex structures makes rational drug design that target Ubc9 possible. Structure-based virtual drug screening has been used increasingly as the first step of drug design to select potential lead templates. This review analyzes all the interfaces between Ubc9 and its binding partners while also highlighting the possible targeting sites on Ubc9 best suited for virtual screening and drug design.
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