Fig. 5 | Nature Communications

Fig. 5

From: Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations

Fig. 5

BCL-2 surface contacts with either venetoclax, S55746 or BaxBH3 peptide. Structure of BCL-2 G101V with a Venetoclax (Ven) or b S55746, or c BCL-2 WT with a BaxBH3 peptide. BCL-2 surface contacts are coloured according to interactions with venetoclax (orange), S55746 (magenta) or BaxBH3 peptide (slate). Key BCL-2 binding pockets (P1 through P4) indicated for each compound and hydrophobic (ϕ) 1–4 residues (L, L, I, L) from the BaxBH3 peptide. c BCL-2 surface contacts with venetoclax are coloured in orange and with BaxBH3 peptide in slate highlighting the increased surface contact area of BaxBH3 relative to venetoclax (PDB id 2XA0)

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