Selectivity by Small-Molecule Inhibitors of Protein Interactions Can Be Driven by Protein Surface Fluctuations
Fig 4
Maps of “pocket space” sampled by individual Bcl-2 family members.
The ensemble of pockets observed from simulation: individual conformations are represented as points on a two-dimensional projection that reflects the pairwise distances between their exemplars. The relative position of exemplars from experimentally-derived Bcl-xL unbound (“U”) and peptide-bound (“P”) structures are indicated, as are the positions of exemplars from Bcl-xL structures solved in complex with various inhibitors (numbers correspond to complexes listed in S1 Table). Exemplars marked “D” correspond to the same “distinct” conformations described in Fig. 5.