Journal of Computations & Modelling

In Silico Docking Analysis of Rat γ-Crystallin Surfaces

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• Abstract

  In silico methods are useful for predicting 3D structure of binding sites when experimental information is lack. The complex interaction between γ-crystallins and small ligands is a key element in understanding the lens transparency. In spite of the high sequence similarity of γ-crystallins, different numbers of pockets were automatically identified on their molecular surfaces. γC-crystallin has the largest binding pocket among rat γ-crystallin individuals. The binding affinities of five putative chemical ligands against the active sites of γ-crystallin proteins were determined by Autodock 4.2. Molecular docking indicated multiple binding modes of such ligands into γ-crystallins pockets.