Molecular perspectives on p97–VCP: progress in understanding its structure and diverse biological functions
Q Wang, C Song, CCH Li - Journal of structural biology, 2004 - Elsevier
The 97-kDa valosin-containing protein (p97 or VCP) is a type-II AAA (A TPases a ssociated
with a variety of a ctivities) ATPases, which are characterized by possessing two conserved
ATPase domains. VCP forms a stable homo-hexameric structure, and this two-tier ring-
shaped complex acts as a molecular chaperone that mediates many seemingly unrelated
cellular activities. The involvement of VCP in the ubiquitin-proteasome degradation pathway
and the identification of VCP cofactors provided us important clues to the understanding of …
with a variety of a ctivities) ATPases, which are characterized by possessing two conserved
ATPase domains. VCP forms a stable homo-hexameric structure, and this two-tier ring-
shaped complex acts as a molecular chaperone that mediates many seemingly unrelated
cellular activities. The involvement of VCP in the ubiquitin-proteasome degradation pathway
and the identification of VCP cofactors provided us important clues to the understanding of …