Premium
Blind docking of drug‐sized compounds to proteins with up to a thousand residues
Author(s) -
Hetényi Csaba,
van der Spoel David
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.01.074
Subject(s) - docking (animal) , amino acid residue , protein–ligand docking , chemistry , drug design , computational biology , drug , plasma protein binding , binding site , amino acid , drug discovery , biochemistry , stereochemistry , combinatorial chemistry , peptide sequence , biology , pharmacology , virtual screening , medicine , nursing , gene
Blind docking was introduced for the detection of possible binding sites and modes of peptide ligands by scanning the entire surface of protein targets. In the present study, the method is tested on a group of drug‐sized compounds and proteins with up to a thousand amino acid residues. Both proteins from complex structures and ligand‐free proteins were used as targets. Robustness, limitations and future perspectives of the method are discussed. It is concluded that blind docking can be used for unbiased mapping of the binding patterns of drug candidates.