Sequence analysis and molecular docking of MMP14
(0) Cancer is a kind of disease which is seriously harmful to human life and health. Among all the tumor associated target proteins, MMPs play a key role in tumor metagenesis and development. Therefore MMP14 is especially interested in our lab for its characteristics of membrane-type expression and its important role in tumor invasions. Here ClustalX, RasMol, TreeView and other kinds of bioinformatics softwares on websites were used to complete the analysis. Transmembrane domain, signal peptide and subcellular localization were predicted respectively by TMHMM 2.0 Server SignalP 3.0 Server PSORT II; Secondary structure of protein was predicted by Jpred and SOPMA server; Tertiary structure of protein was predicted by SWISS-MODEL and Accelrys Discovery Studio; Docking of the specific MMP14 binding peptides selected from phage display peptides library and cell subtraction biopanning was completed by Molegro Virtual Docker. Similar substrate specificity can be made from the analysis of the eight species (Homo sapiens, Rat, Mus musculus, Canis familiaris, Eqqus caballus, Bovin and Xenopus laevis) of MMP14 which contains a good conservative domain of a HX domain; by molecular docking, it was found that the docking location sites between all predicted peptide motifs and MMP14 were at aa. 121 -123 (His-Asn-Glu) in the MMP14 indicating that all selected peptides were directed against MMP14 target protein on MG-63 cell surface rather than other proteins. At the same time, it was obvious that His-Asn-Glu was very likely to be an important target domain for the selected MMP14 inhibitors. On the other hand, due to the target sequences were rightly at the Zn ion binding site, the study of the target sequence became especially important.
Zhijuan Liang Jingshuang Huang Canquan Mao
Laboratory of Molecular Evolution and Applied Biology, School of Life Science and Engineering, Southwest Jiaotong University, Chengdu, 610031
国际会议
武汉
英文
247-248
2010-09-01（万方平台首次上网日期，不代表论文的发表时间）