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. 2015 Jun 8;112(26):7984–7989. doi: 10.1073/pnas.1424108112

Fig. 7.

Fig. 7.

The M114T mutation causes a surface-exposed pocket to expand into the core of the PFN1 protein. (A) Residues are depicted as described in Fig. 3. The van der Waals radii of residues 90, 114, and 18 are in contact in the PFN1 WT structure (Top). These contacts are reduced by the M114T mutation (Bottom) owing to the smaller size of threonine, leading to an enlargement of the surface-exposed pocket. (B) PFN1 WT is shown with a transparent surface and the secondary structure is shown in cartoon representation. The surface pocket volume for PFN1 WT (green) and the cleft volume for PFN1 M114T chain B (red) are depicted as opaque surfaces and were generated using SiteMap. The predicted cavity (blue) for PFN1 C71G (generated using PyMOL) overlays with the M114T void, and unlike the WT and M114T volumes, is not surface-exposed. The insets (Right) show the aforementioned voids for WT (Top), M114T chain B (Middle), and C71G (Bottom).