The 3D structure of the defense-related rice protein Pir7b predicted by homology modeling and ligand binding studies
To better understand the ligand-binding mechanism of protein Pir7b, important part in detoxification of a pathogen-derived compound against Pyricularia oryzae, a 3D structure model of protein Pir7b was constructed based on the structure of the template SABP2. Three substrates were docking to this protein, two of them were proved to be active, and some critical residues are identified, which had not been confirmed by the experiments. His87 and Leu17considered as oxyanion hole contribute to initiating the Ser86 nucleophilic attack. Gln187 and Asp139 can form hydrogen bonds with the anilid group to maintain the active binding orientation with the substrates. The docking model can well interpret the specificity of protein Pir7b towards the anilid moiety of the substrates and provide valuable structure information about the ligand binding to protein Pir7b.
Defense-related esterase Homology modeling Ligand selectivity Molecular docking Pir7b
Quan Luo Wei-Wei Han Yi-Han Zhou Yuan Yao Ze-Sheng Li
State Key Laboratory of Theoretical and Computational Chemistry,Institute of Theoretical Chemistry, Jilin University,Changchun 130023, Peoples Republic of China
国际会议
广州
英文
41-51
2008-11-01（万方平台首次上网日期，不代表论文的发表时间）