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Fig. 2 | Cell Communication and Signaling

Fig. 2

From: Bacterial serine protease HtrA as a promising new target for antimicrobial therapy?

Fig. 2

Structural model of the H.pylori HtrA monomer. The model is based on a preliminary X-ray crystal structure of the apo-enzyme containing one of the two PDZ domains [63]. The cartoon structure (a) shows the protease domain with the catalytic residue Ser221 highlighted. The interface between the protease domain and PDZ1 is mediated by helix-helix interactions. The surface representation (b) has the same orientation as in (a). Temperature coloring is according to the computed “ligandability” [45, 64]. A potential ligand interaction “hot spot” is predicted inside the active site (approximated by the dashed circle). This model and related computational analyses support the design of H. pylori HtrA inhibitors. The graphics were prepared with MacPyMol (v1.7, Schrödinger LLC, New York, NY, USA)

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