Figure 2
From: Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator
The antiparallel-to-parallel equilibrium. (a) Structural comparison of the C-terminal β-barrel between human apo-uPA (pink) and apo-muPA (blue) displaying the 180-degree switch of the β9-strand. Key residues of the S1 specificity pocket (Asp189), the activation pocket (Asp194 and Ile16), and the Cys168-Cys182 and Cys191-Cys220 disulfide bridges are shown as sticks. (b) SDS-PAGE analysis of apo-muPA from the protein stock used for the crystallization experiments or from the washed and dissolved apo-muPA crystals in the absence or presence of PAI-1.
