de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Self-compartmentalizing proteases

MPS-Authors
There are no MPG-Authors available
Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Lupas, A., Flanagan, J. M., Tamura, T., & Baumeister, W. (1997). Self-compartmentalizing proteases. Trends in Biochemical Sciences, 22(10), 399-404.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-727E-2
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. [References: 58]