Sequence and structure of the coronavirus peplomer protein.

de Groot, R. J.; Lenstra, J. A.; Luytjes, W.; Niesters, H. G.; Horzinek, M. C.; van der Zeijst, B. A.; Spaan, W. J.

doi:https://doi.org/10.1007/978-1-4684-1280-2_4

Sequence and structure of the coronavirus peplomer protein.

DSpace/Manakin Repository

Sequence and structure of the coronavirus peplomer protein.

de Groot, R. J.; Lenstra, J. A.; Luytjes, W.; Niesters, H. G.; Horzinek, M. C.; van der Zeijst, B. A.; Spaan, W. J.

(1987) Coronaviruses, pp. 31 - 38
Advances in Experimental Medicine and Biology, pp. 31 - 38

(Part of book)

Abstract

Coronaviruses display a characteristic fringe of large (17–20 nm), clubshaped peplomers, each consisting of a di- or trimer of the peplomer protein (Cavanagh et al. 1983). The peplomer protein, E2, plays an important role during the infection proces. It mediates the binding of virions to the host-cell receptors and is ... read more

Download/Full Text

Open Access version via Utrecht University Repository

Publisher version

Keywords: Infectious Bronchitis Virus, Coiled Coil, Heptad Repeat, Mouse Hepatitis Virus, Infectious Bronchitis Virus Strain, General Biochemistry,Genetics and Molecular Biology

DOI: https://doi.org/10.1007/978-1-4684-1280-2_4

ISSN: 0065-2598

Publisher: Springer, Springer

(Peer reviewed)

See more statistics about this item