- Oral presentation
- Open Access
Variation of geometrical and physicochemical properties in protein binding pockets and their ligands
© Kahraman et al; licensee BioMed Central Ltd. 2007
- Published: 20 November 2007
- Harmonic Function
- Electrostatic Potential
- Binding Pocket
- Match Algorithm
- Molecular Recognition
Physicochemical complementarity is commonly believed to be the driving force for molecular binding. The complementarity for example of electrostatic potentials is regarded as the force that draws the ligand from the solvent into the binding site . If this hypothesis is true, the same ligand should encounter complementarity environmental properties in all proteins to which it binds. We have used our recently published ligand and binding pocket matching algorithm  to test this common assumption by searching for property distributions that are similar for the same ligand bound to different proteins.
The algorithm bases on real spherical harmonic functions, which are applicable to approximate any property function on a unit sphere. These property functions can either be of geometrical or physicochemical nature. For our current analysis we used the shape of binding pockets to test their geometrical similarity and mapped electrostatic, van der Waals and hydrophobicity potentials of the protein on the ligand surface to simulate the physicochemical forces that a ligand may feel in its binding site.
These results demonstrate that binding sites that bind the same ligand can exhibit a large variation of properties by facing different physicochemical forces within different binding sites. The results urge a re-evaluation of the total contribution of some physicochemical properties to molecular recognition and the factors that drive molecular binding.
The molecules in the figure were rendered using PyMOL (W.L. DeLano, http://pymol.sourceforge.net/).
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This article is published under license to BioMed Central Ltd.