CHED 841 |
| Zinc Finger Antiviral Protein (ZAP), discovered in 2002, has been shown to increase resistance to infection by Moloney Murine Leukemia virus and Sindbis virus by more than thirty fold. ZAP functions by degrading viral mRNA in the host cell cytoplasm without influencing the host mRNA levels. The structure of the N-terminal zinc binding domain of ZAP is critical in the interactions it has with the viral RNA. The goal of our research is to determine the structure of this domain using nuclear magnetic resonance. In order to achieve this, the ZAP zinc binding domain (ZAP-ZBD; residues 1-250) was cloned, and expressed in E.coli. Initial attempts to express ZAP-ZBD using a glutathione-S-transferase fusion protein system resulted in insoluble protein products. Therefore, two other fusion protein systems, Maltose Binding Protein and N-utilization substance-A, were screened to investigate how this would affect production of soluble protein. Optimization of purification conditions is underway. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |