Figure 2
From: Structure of prothrombin in the closed form reveals new details on the mechanism of activation
Intramolecular interactions between kringle-1 and the protease domain. (a) Zoom-in view of the interface between kringle-1 (cartoon, red) and the protease domain (surface, yellow); positively charged residues of loop-1 (Arg90, Arg92 and Lys96) are shown in cyan. Residue Tyr93 in kringle-1 is shown in stick representation while residue Trp547 is colored in magenta. (b) Zoom-in view of the face-to-face interaction between Tyr93 and Trp547 in the structure of proTΔ154-167 solved at 2.2 Å resolution14. The electron density 2Fo- Fc map is countered at 2.0σ. (c) Structural overlay of the catalytic triad (His363, Asp419, Ser525) and Trp547 of proTCC (yellow), proTΔ154-167 (5ED314, cyan), proTΔ146-167 form-1 (4O037, magenta) and proTΔ146-167 form-2 (4NZQ14, green). (d) Binding of fragment-1 to prethrombin-2 monitored by SPR. Two-fold dilutions of fragment-1, from 119 µM to 7.4 µM, were injected over both the active prethrombin-2 surface and an unmodified CM5 surface. Reference-subtracted data is shown in red. Buffer-only injections are shown for the purposes of comparison in black.
