Three dimensional homology modeling of cytochrome P450 2s1(CYP2sl) and docking study on CYP2s1-retinoid acid

By means of homology modeling and molecular dynamics simulation, the three dimensional (3D) structure of CYP2sl was constructed on the basis of the crystal structure of CYP2c5 (PDB:1DT6). The components and conformation of CYP2sl binding site were proposed by using binding-site program and analyzing the binding site of the CYP family binding and catalysis characters. The ligand (retinoid acid) was docked to CYP2sl by using the affinity program, and five conformations with lower energies were collected. By analyzing the complex of CYP2s1-retinoid acid which has the lowest energy among the five collected conformations, we know that nonbonding interaction is the major interaction in the complex, and the residues Glu 411 and Ala 414 play an important role in the binding and catalysis for this enzyme.