TY - JOUR
T1 - Self-compartmentalizing proteases
AU - Lupas, Andrei
AU - Flanagan, John M.
AU - Tamura, Tomohiro
AU - Baumeister, Wolfgang
PY - 1997/10
Y1 - 1997/10
N2 - Among the hundreds of proteases characterized so far, most of which are monomeric or dimeric, there is a small group that form compartments through self-association and that segregate their proteolytic active sites to the interior of these compartments. Although few in number, they represent the main agents of intracellular protein breakdown. They belong to different hydrolase families but have converged towards the same barrel-shaped architecture. Frequently, they are coupled to chaperone-like ATPases of similar quaternary structure that regulate the access to the proteolytic compartments and appear to have been recruited from the same branch of P-loop NTPases.
AB - Among the hundreds of proteases characterized so far, most of which are monomeric or dimeric, there is a small group that form compartments through self-association and that segregate their proteolytic active sites to the interior of these compartments. Although few in number, they represent the main agents of intracellular protein breakdown. They belong to different hydrolase families but have converged towards the same barrel-shaped architecture. Frequently, they are coupled to chaperone-like ATPases of similar quaternary structure that regulate the access to the proteolytic compartments and appear to have been recruited from the same branch of P-loop NTPases.
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U2 - 10.1016/S0968-0004(97)01117-1
DO - 10.1016/S0968-0004(97)01117-1
M3 - Review article
C2 - 9357316
AN - SCOPUS:0030867486
SN - 0968-0004
VL - 22
SP - 399
EP - 404
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 10
ER -