2wpo
From Proteopedia
HCMV PROTEASE INHIBITOR COMPLEX
Overview
Human cytomegalovirus (HCMV) protease belongs to a new class of serine proteases, with a unique polypeptide backbone fold. The crystal structure of the protease in complex with a peptidomimetic inhibitor (based on the natural substrates and covering the P4 to P1' positions) has been determined at 2.7 A resolution. The inhibitor is bound in an extended conformation, forming an anti-parallel beta-sheet with the protease. The P3 and P1 side chains are less accessible to solvent, whereas the P4 and P2 side chains are more exposed. The inhibitor binding mode shows significant similarity to those observed for peptidomimetic inhibitors or substrates of other classes of serine proteases (chymotrypsin and subtilisin). HCMV protease therefore represents example of convergent evolution. In addition, large conformational differences relative to the structure of the free enzyme are observed, which may be important for inhibitor binding.
About this Structure
2WPO is a Single protein structure of sequence from Human herpesvirus 5. Full crystallographic information is available from OCA.
Reference
Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease., Tong L, Qian C, Massariol MJ, Deziel R, Yoakim C, Lagace L, Nat Struct Biol. 1998 Sep;5(9):819-26. PMID:9731777 Page seeded by OCA on Sun May 4 19:10:37 2008
