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English: The structure of the murine polyomavirus capsid protein VP1 in complex with the GT1a glycan. GT1a is shown in yellow and the VP1 monomer with a white surface and a blue protein backbone. A complex network of hydrogen bonds, many water-mediated, is shown at the binding surface, with participating protein residues shown as sticks. Mutations of the two residues shown in cyan at the bottom of the figure can significantly affect pathogenicity.

Rendered from PDB ID 5CPW.

Original paper: Buch MHC, Liaci AM, O’Hara SD, Garcea RL, Neu U, et al. (2015) Structural and Functional Analysis of Murine Polyomavirus Capsid Proteins Establish the Determinants of Ligand Recognition and Pathogenicity. PLoS Pathog 11(10): e1005104. doi: 10.1371/journal.ppat.1005104 http://journals.plos.org/plospathogens/article?id=10.1371%2Fjournal.ppat.1005104
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Author Opabinia regalis

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28 April 2016

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current04:59, 29 April 2016Thumbnail for version as of 04:59, 29 April 20161,260 × 1,120 (1.17 MB)Opabinia regalis{{Information |Description ={{en|1=The structure of the murine polyomavirus capsid protein VP1 in complex with the GT1a glycan. GT1a is shown in yellow and the VP1 monomer with a white surface and a blue protein backbone. A complex network of hydrog...

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