Binding conformations of top-scored compounds from natural products library in the SH2 domain of hSTAT1 and hSTAT3.

<p><b>(A)</b> Binding pose variation of the top-scored hSTAT1-specific inhibitor in SH2 domain of hSTAT1 and hSTAT3. <b>(B)</b> Binding pose variation of the top-scored hSTAT3-specific inhibitor in SH2 domain of hSTAT1 and hSTAT3. The binding pose variations are shown in line representation, colored in blue and violet. Results were obtained using Surflex-Dock 2.6 program.</p

STAT3-CBAVs of STAT3-specific inhibitors.

<p>Graph presents comparative binding affinity values of a selection of STAT3-specific inhibitors docked to models of all hSTAT monomers.</p

Binding conformations of top-scored compounds from clean leads library in the SH2 domain of hSTAT1 and hSTAT3.

<p>(A) Binding pose variation of the top-scored hSTAT1-specific inhibitor in SH2 domain of hSTAT1 and hSTAT3. (B) Binding pose variation of the top-scored hSTAT3-specific inhibitor in SH2 domain of hSTAT1 and hSTAT3. The binding pose variations are shown in line representation, colored in yellow and green. Results were obtained using Surflex-Dock 2.6 program.</p

Structural models and phylogenetic comparison of hSTAT monomers (1, 2, 3, 4, 5A, 5B and 6) with their specific pTyr-linkers.

<p><b>(A)</b> Phylogenetic distribution of hSTATs in form of a simplified phylogenetic tree. <b>(B)</b> Models of the monomers are shown in the cartoon representation with pTyr-peptides in the stick representation. Specific domains are positioned as follows: N-domain on the top-left, coiled-coiled domain on the bottom-center, C-domain on the top-right and SH2 domain on the top-center, to facilitate visual analysis of phosphotyrosine (pTyr)-linker and the SH2 interactions. Monomers are colored according to the predicted local deviation from the real structure (the predicted error of the model), as calculated by MetaMQAP. Blue indicates low predicted deviation of Cα atoms down to 0Å, red indicates unreliable regions with deviation > 5Å, green to orange indicate intermediate values. pTyr-peptides are colored in violet, while pTyr residue is colored in pink. <b>(C)</b> Models of hSTAT dimers with the linker of monomer I in the SH2 domain of monomer II. pTyr-peptides are presented in stick representation, pY+0—pTyr binding pocket, pY-X—hydrophobic side-pocket. SH2 domains are in the surface representation, colored according to the distribution of the electrostatic surface potential, calculated with APBS. Blue indicates positively charged regions, red indicates negatively charged regions.</p

Top-scored binding conformation of stattic in the SH2 domain of all hSTATs.

<p>Stattic is shown in stick representation, pTyr-linker is presented as green colored lines with pTyr residue in pink. Results were obtained using Surflex-Dock 2.6 program.</p

Structure of Trypanosoma Brucei 20S Editosome: theoretical model

<div>Structural model of <i>Trypanosoma Brucei</i> 20S Editosome as of July 2018.<br></div><div><br></div><div>The model was generated using PyRy3D software in november 2016.</div