Fig. 2: Comparison between structural features of WT TPP1, Glu169Δ TPP1, Lys170Δ TPP1, and Leu95Gln TPP1. | Communications Chemistry

Fig. 2: Comparison between structural features of WT TPP1, Glu169Δ TPP1, Lys170Δ TPP1, and Leu95Gln TPP1.

From: Conformational plasticity and allosteric communication networks explain Shelterin protein TPP1 binding to human telomerase

Fig. 2

a Topology of TPP1 and the 3D structure of the OB-domain (gray). TEL-patch and Lys170 are represented through their solvent-accessible surface (yellow and orange, respectively). b Plot of the RMSD as a function of simulation time computed for the secondary structure Cα atoms of WT, Glu169Δ, Lys170Δ, and Leu95Gln TPP1 (gray, green, orange, and cyan, respectively). c Conformations assumed by the TEL-patch in cluster families W1, W2, and W3. The solvent-accessible surface is shown in red, green and blue, respectively. d Conformations assumed by the TEL-patch in cluster families ΔE1 and ΔE2. The solvent-accessible surface is shown in red and green. e Conformations assumed by the TEL-patch in cluster families ΔK1 and ΔK2. The solvent-accessible surface is shown in red and green. f Conformations assumed by the TEL-patch in cluster families LQ1 and LQ2. The solvent-accessible surface is shown in red and green. g Plot of the Solvent Accessible Surface Area (SASA) as a function of simulation time calculated for the TEL-patch in WT, Glu169Δ, Lys170Δ, and Leu95Gln TPP1 (gray, green, orange, and cyan respectively). h Plot of RMSF values computed for each residue of WT, Glu169Δ, Lys170Δ, and Leu95Gln TPP1 (gray, green, orange, and cyan respectively). The TEL-patch’s residues are represented as histograms in the insets.

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