Function
Proteasome (PRTS) are large protein complexes which degrade unneeded proteins into small polypeptides[1]. The 26S PRTS is composed of a central 20S core particle which contains 4 stacked rings each with several members and two 19S caps. The 19S cap is composed of a base with 10 proteins six of which are ATPases and a lid which contains 9 proteins which bind polyubiquitin.
- 13S PRTS is a PRTS core intermediate containing α ring, partial β ring and 3 chaperones[2].
- 15S PRTS is half of an 20S PRTS and upon dimerisation forms the mature 20S PRTS[3].
For more details see 3unb.
Structural highlights
The core particle two outer rings contain 7 α subunits (Y7, Y13, PRE6, PRE5, PUP2, C1, C7-α) which form the PRTS gate. The two inner rings contain 7 β subunits (PRE2, PRE4, PRE3, PUP1, PUP3, C5, C11) with protease activity[4].
3D Structures of Proteasome
Proteasome 3D structures
See Also
PROTAC (Proteolysis-Targeting Chimera), an alternative to conventional enzyme inhibitors, by enabling proteasome induced degradation of the target protein.
