Format

Send to

Choose Destination
Trends Biochem Sci. 1997 Oct;22(10):399-404.

Self-compartmentalizing proteases.

Author information

1
Smithkline Beecham Pharmaceuticals, Collegeville, PA 19426-0989, USA. lupasa00@mh.us.sbphrd.com

Abstract

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.

PMID:
9357316
DOI:
10.1016/s0968-0004(97)01117-1
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center