The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding.

ABSTRACT: The conformational flexibility of target proteins continues to be a major challenge in accurate modeling of protein-inhibitor interactions. A fundamental issue, yet to be clarified, is whether the observed conformational changes are controlled by the protein or induced by the inhibitor. Although the concept of induced fit has been widely adopted for describing the structural changes that accompany ligand binding, there is growing evidence in support of the dominance of proteins' intrinsic dynamics which has been evolutionarily optimized to accommodate its functional interactions. The wealth of structural data for target proteins in the presence of different ligands now permits us to make a critical assessment of the balance between these two effects in selecting the bound forms. We focused

SUBMITTER: Bakan A 

PROVIDER: S-EPMC2728110 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature