Targeting the SUMO E2 conjugating enzyme Ubc9 interaction for anti-cancer drug design.
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.
Duan
Xinyuan
X
James Graham Brown Cancer Center, University of Louisville, 529 South Jackson Street, Louisville, Kentucky, 40202, USA.
Trent
John O
JO
Ye
Hong
H
D000970:Antineoplastic Agents / Q000737:chemistry / Q000494:pharmacology*; D001665:Binding Sites / Q000187:drug effects; D016503:Drug Delivery Systems; D015195:Drug Design; D006801:Humans; D054730:Protein Interaction Domains and Motifs / Q000187:drug effects; D044763:Ubiquitin-Conjugating Enzymes / Q000378:metabolism*; D000098843:Ubiquitin-Conjugating Enzyme UBC9
D000970:Antineoplastic Agents; D044763:Ubiquitin-Conjugating Enzymes; D000098843:Ubiquitin-Conjugating Enzyme UBC9