Structure and network analysis of non-covalent residue interactions for T54

Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of with co-crystallized ligands taken from two superimposed PDB structures: with ligand CPX (yellow) and with ligand SCH 446211 (light blue). Right column: corresponding network analysis of non-covalent residue interactions for T54 mutants. Residues presumed to interact with the cyclopropyl group of VX-950 are indicated by black dots. Nodes represent residues and colored edges represent different types of interactions (see Figure 4): van der Waals interactions, backbone-side chain (blue), side chain-side chain (red); H-bond interactions, backbone-side chain (green), side chain-side chain (orange). Anti-parallel β-sheet and H-bond interactions of T54 with L44 and V55 (yellow). H-bonds are shown as cyan dotted lines and corresponding distances printed in cyan. Loop-forming residues (orange) and hydrophobic pocket conformation. Impact of T54 mutants on the catalytic triad via the node V55 (purple).<p><b>Copyright information:</b></p><p>Taken from "Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus"</p><p>http://genomebiology.com/2008/9/1/R16</p><p>Genome Biology 2008;9(1):R16-R16.</p><p>Published online 23 Jan 2008</p><p>PMCID:PMC2395260.</p><p>