Literature summary for 3.4.21.97 extracted from

Fernandes de Oliveira, C.A.; Werneck Guimaraes, C.R.; Barreiro, G.; Bicca de Alencastro, R.
Human cytomegalovirus protease: Why is the dimer required for catalytic activity? (2007), J. Chem. Theory Comput., 3, 278-288.

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Application

Application	Comment	Organism
additional information	conformational changes of the dimer upon covalent binding reproduced by molecular dynamics simulations of the noncovalent complex model, demonstrating that the HCMV protease operates by an induced-fit mechanism. Catalytic activity of the dimer is a result of more favorable interactions between the oxyanion in the covalently bound state and the backbone nitrogen of Arg165	Human betaherpesvirus 5

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of HCMV protease in complex with the peptidomimetic inhibitor BILC 821 as protease model. Only the dimeric form of the protease is able to reorient the main-chain atoms of Arg165 along the reaction coordinate in order to stabilize more efficiently the oxyanion formed in the reaction pathway	Human betaherpesvirus 5

Inhibitors

Inhibitors	Comment	Organism	Structure
BILC 821	-	Human betaherpesvirus 5

Organism

Organism	UniProt	Comment	Textmining
Human betaherpesvirus 5	-	-	-

Subunits

Subunits	Comment	Organism
homodimer	crystallography	Human betaherpesvirus 5

Synonyms

Synonyms	Comment	Organism
HCMV protease	-	Human betaherpesvirus 5
human cytomegalovirus protease	-	Human betaherpesvirus 5

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Release 2023.1 (January 2023)