Proteasome

spinqualitylabelsall models Yeast proteasome 20S core complex with salinosporamide derivative, 3gpt Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Proteasome (PRTS) are large protein complexes which degrade unneeded proteins into small polypeptides. 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. 15S PRTS is half of an 20S PRTS and upon dimerisation forms the mature 20S PRTS. 19S PRTS is the regulatory paricle pf PRTS which recognizes the ubiquinated substrates destined for proteolysis. Immunoproteasome is PRTS variant induced by inflammation. Preholoproteasome is created by the fusion of 2 half 20S particles yielding an immature PRTS. 20S PRTS Pre1-1 mutation is yeast PRTS variant which prevents PRTS maturation. 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. α subunits and β subunits. Salinosporamide derivative binding site of chain H. Covalent bond between Salinosporamide derivative and Thr1. 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.

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky, Joel L. Sussman, Michal Harel