Spatial chemical conservation of hot spot interactions in protein-protein complexes-1

<p><b>Copyright information:</b></p><p>Taken from "Spatial chemical conservation of hot spot interactions in protein-protein complexes"</p><p>http://www.biomedcentral.com/1741-7007/5/43</p><p>BMC Biology 2007;5():43-43.</p><p>Published online 9 Oct 2007</p><p>PMCID:PMC2231411.</p><p></p> dots [51]) and the pseudocenters (balls). Only surface exposed pseudocenters are considered. Hydrogen bond donors are blue, acceptors – red, donors/acceptors – green, and aromatic – white. The right figure illustrates the definition of pseudocenters and the bar at the bottom illustrates the complementarity of the pseudocenter properties. () Alignment of 6 PPIs of serine proteases with inhibitors. The trypsins (1cbwHG, 1tawA, 1ca0HG) are gray and the subtilisins (1cseE, 2sicE, 1oyvB) are blue. The corresponding inhibitors (1cbwI, 1tawI, 1ca0I, 1cseI, 2sicI, 1oyvI) are colored ranging from yellow to purple respectively. The right figure presents the 9 spatially conserved interactions (purple arrows). The catalytic residues of the serine proteases (gray sticks) were recognized to form 5 similar interactions (3 hydrogen bonds, 1 hydrophobic aliphatic and 1 aromatic) with the corresponding hot spots of the inhibitors K15(1cbw), R15(1taw,1ca0), K45(1cse), M73(2sic) and R5(1oyv). These residues, which have different amino acid identities and backbone locations are represented as black sticks

Spatial chemical conservation of hot spot interactions in protein-protein complexes-0

<p><b>Copyright information:</b></p><p>Taken from "Spatial chemical conservation of hot spot interactions in protein-protein complexes"</p><p>http://www.biomedcentral.com/1741-7007/5/43</p><p>BMC Biology 2007;5():43-43.</p><p>Published online 9 Oct 2007</p><p>PMCID:PMC2231411.</p><p></p> dots [51]) and the pseudocenters (balls). Only surface exposed pseudocenters are considered. Hydrogen bond donors are blue, acceptors – red, donors/acceptors – green, and aromatic – white. The right figure illustrates the definition of pseudocenters and the bar at the bottom illustrates the complementarity of the pseudocenter properties. () Alignment of 6 PPIs of serine proteases with inhibitors. The trypsins (1cbwHG, 1tawA, 1ca0HG) are gray and the subtilisins (1cseE, 2sicE, 1oyvB) are blue. The corresponding inhibitors (1cbwI, 1tawI, 1ca0I, 1cseI, 2sicI, 1oyvI) are colored ranging from yellow to purple respectively. The right figure presents the 9 spatially conserved interactions (purple arrows). The catalytic residues of the serine proteases (gray sticks) were recognized to form 5 similar interactions (3 hydrogen bonds, 1 hydrophobic aliphatic and 1 aromatic) with the corresponding hot spots of the inhibitors K15(1cbw), R15(1taw,1ca0), K45(1cse), M73(2sic) and R5(1oyv). These residues, which have different amino acid identities and backbone locations are represented as black sticks