ENRI: A tool for selecting structure-based virtual screening target conformations

被引:12
作者
Akbar, Rahmad [1 ]
Jusoh, Siti Azma [2 ,3 ]
Amaro, Rommie E. [2 ]
Helms, Volkhard [1 ]
机构
[1] Saarland Univ, Ctr Bioinformat, Saarbrucken, Germany
[2] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
[3] Univ Teknol MARA Malaysia, Fac Pharm, Bandar Puncak Alam, Selangor, Malaysia
关键词
binding pocket; classification; conformational dynamics; molecular docking; molecular dynamics simulation; virtual screening; BINDING-SITES; DRUGGABILITY; POCKETS; PREDICTION; LIGANDS; SHAPE;
D O I
10.1111/cbdd.12900
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Finding pharmaceutically relevant target conformations from an arbitrary set of protein conformations remains a challenge in structure-based virtual screening (SBVS). The growth in the number of available conformations, either experimentally determined or computationally derived, obscures the situation further. While the inflated conformation space potentially contains viable druggable targets, the increase of conformational complexity, as a consequence, poses a selection problem. To address this challenge, we took advantage of machine learning methods, namely an over-sampling and a binary classification procedure, and present a novel method to select druggable receptor conformations. Specifically, we trained a binary classifier on a set of nuclear receptor conformations, wherein each conformation was labeled with an enrichment measure for a corresponding SBVS. The classifier enabled us to formulate suggestions and identify enriching SBVS targets for six of seven nuclear receptors. Further, the classifier can be extended to other proteins of interest simply by feeding new training data sets to the classifier. Our work, thus, provides a methodology to identify pharmaceutically interesting receptor conformations for nuclear receptors and other drug targets.
引用
收藏
页码:762 / 771
页数:10
相关论文
共 29 条
[1]
Notes of a protein crystallographer: on the high-resolution structure of the PDB growth rate [J].
Abad-Zapatero, Cele .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2012, 68 :613-617
[2]
[Anonymous], 2015, MAESTR 9 4
[3]
GROMACS - A MESSAGE-PASSING PARALLEL MOLECULAR-DYNAMICS IMPLEMENTATION [J].
BERENDSEN, HJC ;
VANDERSPOEL, D ;
VANDRUNEN, R .
COMPUTER PHYSICS COMMUNICATIONS, 1995, 91 (1-3) :43-56
[4]
Bolton EE, 2010, ANN REP COMP CHEM, V4, P217, DOI 10.1016/S1574-1400(08)00012-1
[5]
Breiman F, 1984, OLSHEN STONE CLASSIF
[6]
Structure-based maximal affinity model predicts small-molecule druggability [J].
Cheng, Alan C. ;
Coleman, Ryan G. ;
Smyth, Kathleen T. ;
Cao, Qing ;
Soulard, Patricia ;
Caffrey, Daniel R. ;
Salzberg, Anna C. ;
Huang, Enoch S. .
NATURE BIOTECHNOLOGY, 2007, 25 (01) :71-75
[7]
CORTES C, 1995, MACH LEARN, V20, P273, DOI 10.1023/A:1022627411411
[8]
Daura X, 1999, PROTEINS, V34, P269, DOI 10.1002/(SICI)1097-0134(19990215)34:3<269::AID-PROT1>3.0.CO
[9]
2-3
[10]
POVME 2.0: An Enhanced Tool for Determining Pocket Shape and Volume Characteristics [J].
Durrant, Jacob D. ;
Votapka, Lane ;
Sorensen, Jesper ;
Amaro, Rommie E. .
JOURNAL OF CHEMICAL THEORY AND COMPUTATION, 2014, 10 (11) :5047-5056