The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment

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Abstract

Intact influenza A virions were bombarded with thermally activated tritium atoms, and the intramolecular distribution of the label in the matrix protein M1 was analyzed to determine the in situ accessibility of its tryptic fragments. These data were combined with the previously reported x-ray crystal structure of the M1 fragment 2-158 [Sha, B. and Luo, M. (1997) Nat. Struct. Biol. 4, 239-244] and the predicted topology of the C domain (159- 252) to propose a model of M1 arrangement in the virus particle.

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Shishkov, A. V., Goldanskii, V. I., Baratova, L. A., Fedorova, N. V., Ksenofontov, A. L., Zhirnov, O. P., & Galkin, A. V. (1999). The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment. Proceedings of the National Academy of Sciences of the United States of America, 96(14), 7827–7830. https://doi.org/10.1073/pnas.96.14.7827

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