1. Analysis of LC8-binding and nonbinding motifs reveals distinct positional preferences.
Analysis of LC8-binding and nonbinding motifs reveals distinct positional preferences. (A) Motif preferences for LC8 binding partners. “Ф” denotes hydrophobic residues; “X” signifies any residue (unless certain residues are disfavored); underlined “X” signifies any residue but with strong preferences for particular residues; “+” denotes positively charged amino acids. Physiochemical properties beneficial for binding are colored dark blue or light blue, based on magnitude, and deleterious properties are colored in red. (B) All known tightly binding sequences (Kd < 10 μM) are cropped to 8 amino acid motifs and built using the Chimera molecular modeling software. This includes LC8 sequences found on the LC8Hub database, and those determined in this article. (C) Overlay of all nonbinding peptides used in this study. Residues are colored based upon whether they are beneficial (blue), deleterious (red), or neutral (white) for binding, using the amino acid enrichment and depletion in known motifs (Fig 6A). (D) Categories of nonbinding sequences. Residues highlighted in red depict the reason the sequence is placed within a given category. *Denotes sequences placed in multiple categories.
Nathan Jespersen et al. LSA 2019;2:e
© 2019 Jespersen et al.