@article {6335,
	title = {Atomic model of an infectious rotavirus particle.},
	journal = {The EMBO Journal},
	volume = {30},
	year = {2011},
	month = {2011 Jan 19},
	pages = {408-16},
	abstract = {<p>Non-enveloped viruses of different types have evolved distinct mechanisms for penetrating a cellular membrane during infection. Rotavirus penetration appears to occur by a process resembling enveloped-virus fusion: membrane distortion linked to conformational changes in a viral protein. Evidence for such a mechanism comes from crystallographic analyses of fragments of VP4, the rotavirus-penetration protein, and infectivity analyses of structure-based VP4 mutants. We describe here the structure of an infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle analysis at about 4.3 {\r A} resolution. The cryoEM image reconstruction permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side chains. It shows how the two subfragments of VP4 (VP8(*) and VP5(*)) retain their association after proteolytic cleavage, reveals multiple structural roles for the β-barrel domain of VP5(*), and specifies interactions of VP4 with other capsid proteins. The virion model allows us to integrate structural and functional information into a coherent mechanism for rotavirus entry.</p>
},
	keywords = {Capsid Proteins, Cell Membrane, Cryoelectron Microscopy, Crystallography, Models, Molecular, Protein Structure, Rotavirus, Secondary, Virion, Virus Internalization},
	issn = {1460-2075},
	doi = {10.1038/emboj.2010.322},
	author = {Settembre, Ethan C and Chen, James Z and Dormitzer, Philip R and Grigorieff, Nikolaus and Harrison, Stephen C}
}
