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The Mechanism of Ubiquitination in the Cullin-RING E3 Ligase Machinery: Conformational Control of Substrate Orientation

Figure 5

Conserved prolines in the linker region.

(A) Skp2 proline puckering up and down is coupled with backbone conformational change. Two snapshots from simulations with prolines puckering up and down were superimposed and the backbone rotations are shown. (B) Superposition of pVHL (Cyan), SOCS2 (pink), and SOCS4 (orange) box domain with prolines at the linker. (C) Superposition of Skp2 (Cyan), Fbw7 (pink), β-TrCP1 (orange), Cdc4 (yellow), Fbs1 (purple) and TIR1 (green) with prolines at the linker. (D) Sequence alignment of pVHL, SOCS2 and SOCS4. (E) Sequence alignment of Skp2, Fbw7, β-TrCP1, Cdc4, Fbs1 and TIR1.

Figure 5

doi: https://doi.org/10.1371/journal.pcbi.1000527.g005