Structural highlights
Function
PSA2_YEAST The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Publication Abstract from PubMed
Despite their structural similarity, the natural products omuralide and vibralactone have different biological targets. While omuralide blocks the chymotryptic activity of the proteasome with an IC50 value of 47 nM, vibralactone does not have any effect at this protease up to a concentration of 1 mM. Activity-based protein profiling in HeLa cells revealed that the major targets of vibralactone are APT1 and APT2.
Omuralide and Vibralactone: Differences in the Proteasome- beta-Lactone-gamma-Lactam Binding Scaffold Alter Target Preferences.,List A, Zeiler E, Gallastegui N, Rusch M, Hedberg C, Sieber SA, Groll M Angew Chem Int Ed Engl. 2013 Nov 28. doi: 10.1002/anie.201308567. PMID:24285701[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ List A, Zeiler E, Gallastegui N, Rusch M, Hedberg C, Sieber SA, Groll M. Omuralide and Vibralactone: Differences in the Proteasome- beta-Lactone-gamma-Lactam Binding Scaffold Alter Target Preferences. Angew Chem Int Ed Engl. 2013 Nov 28. doi: 10.1002/anie.201308567. PMID:24285701 doi:http://dx.doi.org/10.1002/anie.201308567
