Journal
STRUCTURE
Volume 13, Issue 10, Pages 1545-1557Publisher
CELL PRESS
DOI: 10.1016/j.str.2005.07.012
Keywords
-
Funding
- NCI NIH HHS [R37 CA013202, R01 CA013202, R01 CA13202] Funding Source: Medline
- NIAID NIH HHS [R01 AI46440, R01 AI047904, R01 AI046440, R01 AI47904, P01 AI045976] Funding Source: Medline
- NIGMS NIH HHS [R01 GM33050, R01 GM62580, R37 GM033050, R01 GM033050, P01 GM062580] Funding Source: Medline
Ask authors/readers for more resources
Reovirus is a useful model for addressing the molecular basis of membrane penetration by one of the larger nonenveloped animal viruses. We now report the structure of the reovirus virion at 7.0 angstrom resolution as obtained by electron cryomicroscopy and three-dimensional image reconstruction. Several features of the myristoylated outer capsid protein mu 1, not seen in a previous X-ray crystal structure of the mu 1-sigma 3 heterohexamer, are evident in the virion. These features appear to be important for stabilizing the outer capsid, regulating the conformational changes in mu 1 that accompany perforation of target membranes, and contributing directly to membrane penetration during cell entry.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available