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. 2017 Mar 18;142:37–54. doi: 10.1016/j.antiviral.2017.03.007

Fig. 4.

Fig. 4

The Frequency of CRD Amino Acid Residues in Antiviral Lectins. Lectins CRDs defined through NMR titration or x-ray co-crystallization experiments were analyzed for their frequency. A total of 84 residues from 17 lectins were used in the analysis. Aspartate and Glutamine were the most commonly found residues across all lectins reviewed. The hydrophobic residues participate in hydrogen bonding through their carbonyl and/or amide atoms. Tyrosine and tryptophan participate in both back bone and side chain interactions in some lectins. Note: If no experimental results are available for residues involved in glycan binding, then the lectin was excluded from the analysis.