Fig. 26.3 The catalytic domains of kinases all have the same folding. The N-terminal domain is composed of five β-pleat...
Fig. 26.4 Based on the crystal structure of a cAMP-dependent kinase with a bound ADP and aluminum trifluoride as a trans...
Fig. 26.7 The kinases p38α and p38β have threonine (Thr106, violet) as gatekeeper residues; a sterically more demandin...
Fig. 26.9 Kinases go through multiple conformations during their activation from an inactive (red) to an active (green) ...
Fig. 26.12 Superimposed crystal structures of Imatinib 26.5 and Tetrahydrostaurosporine 26.27 (Fig. 26.13) with the acti...
Fig. 26.17 Superposition of the crystal structures of the complex of PIM-1 kinase with the unselective inhibitor stauros...
Fig. 26.19 The crystallographically determined binding mode of a phosphorylated tyrosine (26.39, green, Fig. 26.21) as a...
Fig. 26.20 (a) Binding mode of the substrate-analogous phosphotyrosine (26.39, Fig. 26.21) in human PTP-1B. The phosphat...
Fig. 26.22 A new allosteric binding site was discovered at Sunesis that is approximately 20 Å away from the catalytic s...
Fig. 26.23 (a) When no phosphorylated substrate is present, the Shp2 phosphatase is self-inhibited by its N-SH2 domain. ...
Fig. 26.24 Crystal structure of full-length Shp2 phosphatase in the inactive form autoinhibited by the N-SH2 domain. The...
Fig. 26.25 The crystals structure of COMT with the cofactor S-adenosyl-L-methionine 26.55 (and the catecholamine-analog...
Fig. 26.27 Superposition of the crystal structures of COMT with SAM 26.55(purple carbon atoms) and the catecholamine-li...
Fig. 26.28 Farnesyldiphosphate 26.65 binds to FTase and occupies a part of the large catalytic site. The crystal structu...