Event Title
Co-Crystallization of Human Cdc7-Dbf4
Presentation Type
Poster/Portfolio
Presenter Major(s)
Cell and Molecular Biology, Biomedical Sciences
Mentor Information
Brad Wallar
Department
Chemistry
Location
Henry Hall Atrium 100
Start Date
11-4-2012 9:00 AM
Keywords
Health, Life Science
Abstract
Cdc7-Dbf4 (DDK) is a two-subunit protein required for DNA replication. This protein is overexpressed in cancer cells and thus could be an important therapeutic target. The goal of this project is to purify significant amounts of DDK for crystallization with stabilizing inhibitors to gain structural information about the DDK-inhibitor complex. Stabilizing inhibitors are important for crystallography because they help create a homogenous sample of protein, making it more likely for crystals to form. An optimized and truncated version of DDK was purified and used for crystallography screening. However, heterogeneity of the complex due to autophosphorylation prevented crystallization. Currently, we are optimizing the purification of DDK to yield untagged and dephosphorylated protein for future crystallography screens. The crystallization of DDK will provide us with the foundation to crystallize DDK-inhibitor complexes, which will aid in the potential design of other inhibitory ligands.
Co-Crystallization of Human Cdc7-Dbf4
Henry Hall Atrium 100
Cdc7-Dbf4 (DDK) is a two-subunit protein required for DNA replication. This protein is overexpressed in cancer cells and thus could be an important therapeutic target. The goal of this project is to purify significant amounts of DDK for crystallization with stabilizing inhibitors to gain structural information about the DDK-inhibitor complex. Stabilizing inhibitors are important for crystallography because they help create a homogenous sample of protein, making it more likely for crystals to form. An optimized and truncated version of DDK was purified and used for crystallography screening. However, heterogeneity of the complex due to autophosphorylation prevented crystallization. Currently, we are optimizing the purification of DDK to yield untagged and dephosphorylated protein for future crystallography screens. The crystallization of DDK will provide us with the foundation to crystallize DDK-inhibitor complexes, which will aid in the potential design of other inhibitory ligands.