The protein Anterior gradient 2 (Agr2) is highly expressed in pancreatic ductal adenocarcinoma (PDAC), and plays a role in the spread of pancreatic cancer cells. While Agr2's structure and molecular level role in PDAC remains unknown, the structure of its homologue Agr3 was recently deposited into the PDB bank. The primary goal of this study is to better understand the structure of Agr2 through x-ray crystallography and NMR spectroscopy. To prepare the protein for structural studies, Agr2 was cloned without its 20 N-terminal amino acid signal peptide (Agr2 d20) and without an additional N-terminal 30 amino acids because of low sequence complexity and predicted structural disorder (Agr2 d50). Using bioinformatics, site-directed mutagenesis was also performed to reduce predicted surface entropy. Crystal trials and preliminary HSQC 15N labeled NMR spectra of Agr2 d20 were unsuccessful and indicated the protein formed a dimer in solution. Research with Agr2 d50 will be presented.

Structural characterization of antierior gradient 2 protein and its role in pancreatic cancer

245th National Meeting (2013)

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