Interactive sequences in the 3D molecular model for αB crystallin.

<p>(A) The interactive sequences corresponding to the bioactive peptides in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0011795#pone-0011795-t001" target="_blank">table 1</a> are represented with space filling spheres in the 3D homology model of human αB crystallin. The microtubule interacting sequences ERTIPITRE (blue) in the C-terminus and LTITSSLSSDGV (green) in the β8 strand of the core domain promoted microtubule assembly, while the sequence FISREFHR (orange) in the core domain loop inhibited microtubule assembly <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0011795#pone.0011795-Ghosh1" target="_blank">[15]</a>. (B) In the primary sequence of human αB crystallin the grey letters indicate interactive sequences with no interaction with tubulin and the colors indicate microtubule interactive sequences. The secondary structure, α helix (∼) and β strand (▪), is indicated above the primary sequence. Underlined sequences are sites of subunit-subunit interaction <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0011795#pone.0011795-Ghosh5" target="_blank">[37]</a>. The sequence FISREFHR (orange), which was responsible for inhibiting microtubule assembly, was not involved in the interactions between αB crystallin subunits during complex assembly, while the two sequences responsible for promoting microtubule assembly, ERTIPITRE (blue) and LTITSSLSSDGV (green), were sites of subunit-subunit interaction.