<p>Comparative analysis of structural disorder in the TNFSF members interacting (A and C) and non-interacting with S100 proteins (B and D).</p>

<p>Aligned intrinsic disorder profiles of the interacting (<b>A</b>) and non-interacting cytokines (<b>B</b>). Disorder propensity was evaluated by PONDR^® FIT [<a href="plosone.org/article/info:doi/10.1371/journal.pone.0341400#pone.0341400.ref081" target="_blank">81</a>], and amino acid sequences were aligned using Clustal Omega multiple sequence alignment tool [<a href="plosone.org/article/info:doi/10.1371/journal.pone.0341400#pone.0341400.ref082" target="_blank">82</a>] available at <a href="ebi.ac.uk/jdispatcher/msa/clustalo?stype=protein" target="_blank">ebi.ac.uk/jdispatcher/msa/clustalo?stype=protein</a> [<a href="plosone.org/article/info:doi/10.1371/journal.pone.0341400#pone.0341400.ref064" target="_blank">64</a>].

Aligned 3D structures of the interacting (<b>C</b>) and non-interacting cytokines (<b>D</b>). 3D structural models for all proteins were generated by AlphaFold [<a href="plosone.org/article/info:doi/10.1371/journal.pone.0341400#pone.0341400.ref083" target="_blank">83</a>]. Multiple structural alignment was conducted by SALIGN web server freely accessible to the academic community at <a href="salilab.org/salign" target="_blank">salilab.org/salign</a> [<a href="plosone.org/article/info:doi/10.1371/journal.pone.0341400#pone.0341400.ref084" target="_blank">84</a>].</p>