论文标题
蛋白质 - 小分子对接具有受体灵活性的伊莫尔斯多克
Protein - Small Molecule docking with receptor flexibility in iMOLSDOCK
论文作者
论文摘要
我们早些时候报道了Imolsdock技术，以执行诱导的肽蛋白对接。 Imolsdock使用相互正交的拉丁正方形（MOLS）技术来采样小分子配体的构象和对接姿势以及受体蛋白的柔性残基，并得出最佳的姿势和构象。在本文中，我们报告了在Imolsdock中进行的延伸，以将非肽的小分子配体扩展到受体蛋白。我们用34个蛋白质配体复合物的数据集和非肽小分子作为配体进行了基准测试和验证的Imolsdock。我们还将Imolsdock与其他灵活的受体对接工具Gold V5.2.1和Autodock Vina进行了比较。获得的结果表明，该方法比这两种算法更好，尽管它消耗了更多的计算机时间。 MOLS 2.0的源代码和二进制文件（在GNU较少的通用公共许可下）可以在https://sourceforge.net/projects/mols2-0/files/上免费下载
We have earlier reported the iMOLSDOCK technique to perform induced-fit peptide-protein docking. iMOLSDOCK uses the mutually orthogonal Latin squares (MOLS) technique to sample the conformation and the docking pose of the small molecule ligand and also the flexible residues of the receptor protein, and arrive at the optimum pose and conformation. In this paper we report the extension carried out in iMOLSDOCK to dock nonpeptide small molecule ligands to receptor proteins. We have benchmarked and validated iMOLSDOCK with a dataset of 34 protein-ligand complexes with nonpeptide small molecules as ligands. We have also compared iMOLSDOCK with other flexible receptor docking tools GOLD v5.2.1 and AutoDock Vina. The results obtained show that the method works better than these two algorithms, though it consumes more computer time. The source code and binary of MOLS 2.0 (under a GNU Lesser General Public License) are freely available for download at https://sourceforge.net/projects/mols2-0/files/
