Conformational transitions upon ligand binding: holo-structure prediction from apo conformations.

ABSTRACT: Biological function of proteins is frequently associated with the formation of complexes with small-molecule ligands. Experimental structure determination of such complexes at atomic resolution, however, can be time-consuming and costly. Computational methods for structure prediction of protein/ligand complexes, particularly docking, are as yet restricted by their limited consideration of receptor flexibility, rendering them not applicable for predicting protein/ligand complexes if large conformational changes of the receptor upon ligand binding are involved. Accurate receptor models in the ligand-bound state (holo structures), however, are a prerequisite for successful structure-based drug design. Hence, if only an unbound (apo) structure is available distinct from the ligand-bound confor

SUBMITTER: Seeliger D 

PROVIDER: S-EPMC2796265 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature