2026-10-10T19:15:03Z
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2026-09-29T17:39:09Z
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<p>Comparative analysis of structural disorder in the TNFSF members interacting (A and C) and non-interacting with S100 proteins (B and D).</p>
Victoria A. Rastrygina (25138459)
Evgenia I. Deryusheva (7300229)
Alexey S. Kazakov (6178109)
Andrey S. Sokolov (25138462)
Maria E. Permyakova (25138465)
Ekaterina A. Litus (25138468)
Vladimir N. Uversky (123421)
Eugene A. Permyakov (13802061)
Sergei E. Permyakov (13802058)
Biochemistry
Medicine
Cell Biology
Genetics
Molecular Biology
Chemical Sciences not elsewhere classified
Immunology
Biological Sciences not elsewhere classified
Cancer
Infectious Diseases
s100p evidences involvement
equilibrium dissociation constants
cellular communication mediated
4 − 1bbl
comprises 20 members
treat several autoimmune
div >< p
conserved binding sites
tnfsf members tnf
13 tnfsf members
tnfsf members
used clinically
thereby suppressing
targeting signaling
targeted therapy
soluble forms
s100 proteins
s100 family
potentially important
pleiotropic calcium
p proteins
interaction partners
f89 residue
explored selectivity
cognate receptors
clinical trials
cell proliferation
calcium leads
bone loss
binding proteins
adaptive immunity
24 μm
21 non
2 nm
<p>Aligned intrinsic disorder profiles of the interacting (<b>A</b>) and non-interacting cytokines (<b>B</b>). Disorder propensity was evaluated by PONDR<sup>®</sup> FIT [<a href="http://www.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="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0341400#pone.0341400.ref082" target="_blank">82</a>] available at <a href="https://www.ebi.ac.uk/jdispatcher/msa/clustalo?stype=protein" target="_blank">https://www.ebi.ac.uk/jdispatcher/msa/clustalo?stype=protein</a> [<a href="http://www.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="http://www.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="http://salilab.org/salign" target="_blank">http://salilab.org/salign</a> [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0341400#pone.0341400.ref084" target="_blank">84</a>].</p>
2026-09-29T17:38:55Z
Image
Figure
10.1371/journal.pone.0341400.g009
https://figshare.com/articles/figure/_p_Comparative_analysis_of_structural_disorder_in_the_TNFSF_members_interacting_A_and_C_and_non-interacting_with_S100_proteins_B_and_D_p_/34026971
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