Abstract
The structural information on proteins and their binding cavities including the catalytic domains and allosteric sites is invaluable for protein function studies and rational drug design. Compared to the number of available sequences, the collection of the experimentally determined structures of proteins is limited. The 3D structures of protein usually form the basis of designing of pharmacologically relevant compounds. Thus, the protein databases provide vast quantities of information on different target of varied pathophysiological conditions. On that account, there is a need of computational methods to complement existing repositories by constructing the atomic-level models of drug-protein assemblies that will not be determined experimentally in the near future.
Published Version
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