The Sanderson Group Webpages
Department of Chemistry
Durham University, Durham, UK
Crystal Structure of the Matrix (M) Protein from Respiratory Syncytial Virus
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Money, V. A., McPhee, H. K., Mosely, J. A., Sanderson, J. M. and Yeo, R. P., Proc. Natl. Acad. Sci. U.S.A., 2009, 106, 4441. (link)
Matrix (M) proteins are fundamental components of enveloped viruses, forming a proteinaceous layer that interacts with the membrane envelope. M proteins also play vital roles at key stages of the viral cycle that require significant membrane remodelling, such as budding.
This structure of the full-length M protein from Respiratory Syncytial Virus (RSV), at a resolution of 1.6 Å, shows that it is comprised of two domains of approximately equal size (~14 kDa each) separated by a short unstructured linker. Interesting structural features include a ring of tyrosine residues encircling the C-terminal domain, and a large patch of positive electrostatic potential that extends across both domains and the linker. Both of these features are likely to play significant roles in the function of the protein, which binds to both neutral membranes and membranes with a complementary negative electrostatic potential.