What is it about?
There is experimental evidence that the viral protein NS5 from Zika interacts with a human protein (STAT2), and this leads to a short circuit of an antiviral response pathway known as type I interferon signaling pathway. The little details on how these two proteins may interact are unknown. This lack of information starts with our lack of knowledge of the full structure of the STAT2 human protein. We built using computational strategies the 3D models of these proteins and studied how they interact at the molecular/atomic level.
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Why is it important?
To test the hypothesis of which amino acids may be important for interaction and prepare mutants to evaluate experimentally it is not an easy task without some structural information or other leads. Here we provide a list of possible residues that are the most important for the interaction between the two proteins studied. In addition, we compare the results obtained by two different docking approaches and evaluated how they performed. This is useful for further studies evaluating similar cases.
Perspectives
For me, the importance of this work is that these studies help to cluster or highlight a cluster of promising candidates. These candidates could be proteins, protein-protein interactions, or specific amino acid residues within a particular protein. These findings with further studies may lead to the discovery of novel drug targets or to understand better how a virus with so little proteins can interfere in so many different ways with the host machinery of defense.
Miguel Mendez
Universidad San Francisco de Quito
Read the Original
This page is a summary of: Interaction of ZIKV NS5 and STAT2 Explored by Molecular Modeling, Docking, and Simulations Studies, January 2019, Springer Science + Business Media,
DOI: 10.1007/978-3-030-17935-9_16.
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