Journal: Journal of Virology

Article Title: Structural Basis for Human Norovirus Capsid Binding to Bile Acids

doi: 10.1128/JVI.01581-18

Figure Lengend Snippet: Conservation of the GII bile acid binding pocket. Amino acid sequence alignments of GII capsids were performed using ClustalX (Genetyx software). The conserved P domain residues interacting with bile acid are highlighted in cyan. Variable residues that interacted with the bile acid tail are colored green. The conserved Asp residue (purple) is known to bind to the fucose moiety of HBGAs. Note that only a partial capsid sequence is shown, and the asterisks indicate highly conserved residues.

Article Snippet: Amino acid sequence alignments of GII capsids were performed using ClustalX (Genetyx software).

Techniques: Binding Assay, Sequencing, Software

Journal: The Journal of Biological Chemistry

Article Title: Human MTH3 (NUDT18) Protein Hydrolyzes Oxidized Forms of Guanosine and Deoxyguanosine Diphosphates

doi: 10.1074/jbc.M112.363010

Figure Lengend Snippet: Sequence characteristics of MTH3-related proteins. A, phylogenic tree of human Nudix family proteins. Structural alignment and the construction of a phylogenic tree were performed using the ClustalW program. NUDT1, NUDT15, and NUDT18 (characterized by their structural features) correspond to MTH1, MTH2, and MTH3, respectively, the names of which were assigned on the basis of their similar biochemical activities. B, comparison of the structures of the MutT family proteins. The numbers correspond to the positions of the amino acid residues from the N termini. The positions of the conserved MutT box are shown by shaded boxes. The relative numbers of amino acid residues identical to those of MTH3 are shown to the right of each sequence.

Article Snippet: The primary structures of human Nudix proteins were analyzed using the ClustalW software program, which is equipped with a sequence analysis application, MacVector (MacVector, Inc.).

Techniques: Sequencing, Comparison