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.

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Apr 11th, 9:00 AM

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.