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Solution structure of Mcl‐1 and its complexes

Bcl‐2 family proteins integrate many signaling pathways leading to cell death (apoptosis). Pro‐survival members of this family, such as Mcl‐1, are aberrantly regulated in many cancers. Pro‐survival Bcl‐2 proteins, including Mcl‐1, have a conserved helical fold while the cell killing pro‐apoptotic ‘BH3‐only’ members may have a less well‐ordered structure. We have characterized the structure of Mcl‐1 complexed with its pro‐apoptotic ‘BH3‐only’ partners. As with other pro‐survival proteins, the BH3‐ligand lies in the groove of Mcl‐1 becoming a well‐ordered helix on binding. Our structural analysis indicates the intermolecular interactions in the complexes are a combination of conserved contacts shared with other pro‐survival Bcl‐2 proteins and unique interactions that confer the distinctive binding profile upon Mcl‐1. Analysis of these structures may provide a structural basis for antagonist design.