Abstract:

The three dimensional structure of human serine racemase (hSR) was modeled and refined using homology modeling and molecular dynamics simulation. This model was assessed by profile-3D and procheck, which confirmed that the refined model was reliable. Complex structures of peptide inhibitors with hSR were obtained and investigated through ligand-receptor docking studies by a molecular docking program, affinity. The binding pattern predicted by the affinity module revealed that important residues interacted with the peptide inhibitors and the module provided further refinement of the hSR/inhibitor binding interaction that may be used as a basis for new structure-based design efforts.

Key words: Human serine racemase, Molecular dynamics simulation, Molecular docking, Homology modeling