Gerald Stubbs
Last active: 2/15/2016

Structural comparisons of the aggregates of tobacco mosaic virus protein.

Stubbs G, Warren S, Mandelkow E
J Supramol Struct. 1979 12 (2): 177-83

PMID: 544935 · DOI:10.1002/jss.400120204

The coat protein of tobacco mosaic virus forms numerous aggregates, including the small A-protein, the disk, and two helical forms. The structures of the disk, the helical protein forms, and the virus are compared. Most of the differences are in the conformation of the chain between residues 89 and 113, which lies in the region of protein at the center of the virus, inside the RNA. It is disordered in the disk, but has a fixed conformation in the virus and the protein helices. The differences between the virus and the two helical protein forms are largely in the conformations of arginines and carboxylic acids in this region.

MeSH Terms (8)

Macromolecular Substances Molecular Weight Protein Binding Protein Conformation RNA, Viral Tobacco Mosaic Virus Viral Proteins X-Ray Diffraction

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