Figure 5
Figure 5. Molecular dynamics simulations study of pVHL–ElonginC–ElonginB complex and interaction with HIF1α. (A) Superimposition of wild-type (wt; grey) and mutated pVHL (green) is shown. The wt P138 (violet) and mutated L138 (green) sites and the critical active site residues for the HIF1α peptide (PDB:1LM8)-binding region are depicted. The P138L mutation perturbs pHIF1α interactions with pVHL because of the conformational effect on the W117 and S111 residues (orange) at 2.8 to 4.3 Å distance from mutated L138. (B) Detail superimposition of wt and P138L pVHL in the interaction with HIF1α.

Molecular dynamics simulations study of pVHL–ElonginC–ElonginB complex and interaction with HIF1α. (A) Superimposition of wild-type (wt; grey) and mutated pVHL (green) is shown. The wt P138 (violet) and mutated L138 (green) sites and the critical active site residues for the HIF1α peptide (PDB:1LM8)-binding region are depicted. The P138L mutation perturbs pHIF1α interactions with pVHL because of the conformational effect on the W117 and S111 residues (orange) at 2.8 to 4.3 Å distance from mutated L138. (B) Detail superimposition of wt and P138L pVHL in the interaction with HIF1α.

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