pPR-AP:pAP cleaves the MCP:pPR-AP:pAP Complex

Stable Identifier
R-HSA-9698929
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Human cytomegalovirus
Compartment
Locations in the PathwayBrowser
General
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The maturational protease (PR) processes both pPR-AP and pPR in a pathway that releases PR, pAP, and AP. Although pAP is sufficient for procapsid assembly, self-cleavage of pPR-AP to PR and release of a number of pAP and pPR-AP products are required for proper DNA encapsidation and production of nucleocapsids. Precise protease cleavage steps lead to the release of major capsid protein (MCP), inactivation of the protease, and orchestration of the replacement of the scaffold in procapsids with viral DNA. PR and AP, as well as pAP forms, are completely removed from nucleocapsids into which DNA has been packaged.

Literature References
PubMed ID Title Journal Year
  Fields Virology

Fields, BN, Knipe, DM, Howley, PM, Griffin, DE

  2001
Participants
Participant Of
hasEvent
Catalyst Activity
Catalyst Activity
Title
ATP-dependent peptidase activity of pPR-AP:pAP [nucleoplasm]
Physical Entity
Activity
Disease
Name Identifier Synonyms
viral infectious disease 934 Viral disease, virus infection, virus infection
Authored
Reviewed
Created
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