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Figure 1 | Virology Journal

Figure 1

From: Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1

Figure 1

A and B Organization of the Polar and Hydrophobic faces of the NSP4 crystal structure of the enterotoxic AAH (A and B respectively). A shows the acidic amino acids, D114, E122, E125 and D132 depicted in a maroon color. The basic amino acids K115, R119, R129 and K133 are shown in blue. B shows the hydrophobic amino acids of the AAH of NSP4 I113, L116, V124, L127, I130, Y131 and L134 in purple. C PyMol representations of the hydrophobic face of NSP4-(residues 46-175) and mutants. Amino acids in purple (I113, V124 and Y131) are indicated by arrows represent the wild type NSP4. Eight mutant clones are viewed below the wild type NSP4. The mutations, I113R, V124D and Y131K are orange, and amino acids that are mutated to alanines are shown as blue. To the right of each represented clone, the results of the yeast two hybrid and the peptide binding assays are given.

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