This model represents 1/4 of the 26S proteasome complex: 1/2 α ring (top) and 1/2 β ring (bottom). The 26S proteasome is a protein complex that degrades proteins. It contains a 20S subunit which is made up of 4 rings of α and β subunits in the configuration α-β-β-α. Each ring is composed of 7 subunits with the 2 α rings having identical subunits. This is the same with the 2 β rings. The β5 subunit contains the catalytic active site where the substrate or inhibitor binds. The α subunits recognize the protein for degradation and opens and closes entry to the catalytic site. The β5 active site residues and inhibitor binding pockets are shown in the model. These are the key sites for inhibiting the proteasome. The inhibitor Bortezomib targets the β5 active site and it’s interactions are shown in the model.
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