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. Author manuscript; available in PMC: 2012 Feb 1.
Published in final edited form as: Proteins. 2011 Feb;79(2):417–427. doi: 10.1002/prot.22892

Figure 4. Structure Mapped Control Sites: Static Method.

Figure 4

The control sites identified by the WT iCPM (data from Figure 3) mapped onto the solvent accessible surface. Increasing iCPM values correspond to the color progression: blue → green → orange → red. Allosteric residues are found on the top groove and around the bottom cavity, both of which are adjacent to the dimer interface. In addition, these two locations are connected by an allosteric path that runs along β-strand 6 (boxed in central image). Several residues are marked by dots and labeled; these serve as reference locations along the pathway. The central image is a side view with the β-barrel of each monomer vertically oriented. The top (bottom) image is rotated about the horizontal axis to show the top (bottom) of the structure. In all views, the dimer interface is a vertical plane perpendicular to the page.