Fig. 5: Structural comparison of the bovine iCP with bovine cCP. | Nature Communications

Fig. 5: Structural comparison of the bovine iCP with bovine cCP.

From: Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ

Fig. 5

a Structural superpositions of the three catalytic subunits of the free bovine iCP (with β1i, β2i, and β5i colored yellow, blue, and red, respectively) on the corresponding subunits of the bovine cCP (in gray, PDB ID: 1IRU). The observable conformational changes are indicated by black arrow and dotted ellipsoid or rectangle, which are followed throughout. b Surface property representations of the catalytic pockets of the three enzymatic subunits for free bovine iCP and bovine cCP, with the most distinct residues between β1i and β1 in this region indicated.

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