|Cytomegalovirus Protease At present a wire frame image of the structure of the cytomegalovirus protease is shown below. There are four monomers that make up the tetrameric protease (shades of green and blue). In each monomer you can see the peptide (green, yellow, brown and red). |
The molecule can be rotated at any time by left clicking the mouse on the molecule and dragging the mouse with the left button depressed. Or you can switch on rotation using the buttons below. To return to the original wire-frame structure, use the reload/refresh button on your browser. Human CMV protease is essential for the production of mature infectious virions, as it performs proteolytic processing near the carboxy terminus (M-site) of the viral assembly protein precursor. hCMV protease is a serine protease, although it has little homology to other clans of serine proteases. The crystal structure of hCMV protease at 2.0 angstroms resolution is shown here in association with a peptide that mimics the viral protein to be cleaved. The inhibitor is bound in an extended conformation, forming an anti-parallel beta-sheet with the protease. Ser 132 and His 63 are found in close proximity in the active site. The structure suggests that the third member of the triad is probably His 157. A dimer of the protease with an extensive interface is found in the crystal structure. The two dimers make fewer contacts with each other.