X-ray diffraction analysis and enzyme inhibitor explain the 3D structure of the Zika virus protease
Posted July 11 2016
As part of a research project at the Institute for Pharmacology and Molecular Biotechnology (IPMB), funded by the German Research Foundation (DFG), CellNetworks member Prof. Dr. Christian Klein and Dr. Christoph Nitsche have developed and synthesized an inhibitor which helps clarify the structure of a key protein of the Zika virus at the atomic level.

The DFG project focuses on manufacturing substances which inhibit the protease of flaviviruses – among them the Zika, dengue and West Nile virus – effectively and with high selectivity. These substances stand out due to their strong binding characteristics to their macromolecular target, the protease of viruses, which is essential for its reproduction. According to Prof. Klein, a strong binding is desirable to eliminate the contact points of infectious pathogens. In addition, it facilitates explaining the three-dimensional structure of these molecular complexes, which – in the case of Zika – are made of the enzyme inhibitor and the protease of the virus. The inhibitor-protease complex was also the basis of research at the Institute of Biochemistry at Lübeck University. Scientists there applied the x-ray diffraction analysis to determine the three-dimensional position of the atoms.


Three-dimensional structure of the Zika virus protease (Hilgenfeld et al.)


With their results, which were recently published in Science, the scientists hope to find new impulses for therapeutic approaches.


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