The computer-aided structure-based study of molecular recognition is an important component of structure-based potential ligands screening. The original DOCK algorithm addressed rigid body docking using a geometric matching algorithm to superimpose the ligand onto a negative image of the binding pocket. A representative docking method is used to study these factors, namely, CDOCKER, a molecular dynamics simulated-annealing-based algorithm, which places a unique constraint on the development process. These results indicated that the CSPs could not only recognize the odours but tastes. The result of Northern blot in this study revealed that the CSPSlit was found not only in antennas but also in legs, deantennated heads, thoraces, wings and abdomens. Especially in legs, its specifically high expression suggested that CSPSlit was perhaps functionally associated with contact chemoreception. CSPSlit with preferentially expression in female abdomen but absent in male suggested that CSPSlit might involve in femalespecific chemical senses during mating or oviposition. Homology modeling is based on the assumption that the proteins with similar sequences might have analogous 3D structures. Thus, selection of a suitable template is the first step. The structural characterization of CSPMbraA6 by NMR for the first time; The crystal structure of CSPMbraA6 in complex with one of these compounds, 12-bromo-dodecanol, reveals extensive conformational changes on binding, resulting in the formation of a large cavity filled by three ligand molecules. However, in the absence of an experimentally determined crystal structure, it is generally recognized that homology modeling of proteins is currently the most accurate method for 3D structure prediction. To study the binding mechanism of rhodojaponin IIICSPSlit complex in depth, the best way is to acquire the 3D crystal structure of it. In PDB, CSPMbraA6 was chosen as the template for constructing the 3D model of CSPSlit for it has 52% amino acid sequence identity with CSPSlit. To assess the reasonable of the 3D model of CSPSlit, Ramachandran plot, verify score and molecular dynamic were used and showed positive results. The results of quality assessment suggest that the model of CSPSlit structure is of reasonable quality compared to the crystal structure of the CSPMbraA6 complex. The 3D model of CSPSlit showed that CSPSlit had typical structure of CSPs,six a-helices has been described in 3D structure of CSPSlit, and four of six cysteine residues are conserved in sequence alignments and formed 2 disulphide bridges, which enforce the organization of the helices. All helices are amphiphilic, with the Staurosporine hydrophobic sides formed mostly by leucines and isoleucines. In 3D model of CSPSlit, helices A and B as well as helices D and E form two V shaped structures as a ‘binding pocket’. Helix C is perpendicular to these two planes and positioned in between the four ends of the two V-shaped structures to close one end of this pocket. The final helix is located packed against the external face of the D-E helices and does not take part in the core assembly. This cavity is delimited by the hydrophobic sides of these helices, and therefore well-suited to constitute a binding site for hydrophobic ligands. The interaction energies between the rhodojaponin III and the important residues of CSPSlit are listed in Table 1. The relative values should be meaningful.