Publication: Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization
Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization
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Di Paolo, C., Hefti, H. P., Meli, M., Landis, H., & Pavlovic, J. (1999). Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization. Journal of Biological Chemistry, 274(45), 32071–32078. https://doi.org/10.1074/jbc.274.45.32071
Abstract
Abstract
Abstract
Mx proteins are large GTPases, which play a pivotal role in the interferon type I-mediated response against viral infections. The human MxA inhibits the replication of several RNA viruses and is organized in oligomeric structures. Using two different experimental approaches, the mammalian two-hybrid system and an interaction dependent nuclear translocation approach, three domains in the carboxyl-terminal moiety were identified that are involved in the oligomerization of MxA. The first consists of a carboxyl-terminal amphipathic helix
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Creators (Authors)
- Di Paolo, C
- Hefti, H P
- Meli, M
- Landis, H
- Pavlovic, J
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Citations
Di Paolo, C., Hefti, H. P., Meli, M., Landis, H., & Pavlovic, J. (1999). Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization. Journal of Biological Chemistry, 274(45), 32071–32078. https://doi.org/10.1074/jbc.274.45.32071
