Inherent versus induced protein flexibility: Comparisons within and between apo and holo structures.

ABSTRACT: Understanding how ligand binding influences protein flexibility is important, especially in rational drug design. Protein flexibility upon ligand binding is analyzed herein using 305 proteins with 2369 crystal structures with ligands (holo) and 1679 without (apo). Each protein has at least two apo and two holo structures for analysis. The inherent variation in structures with and without ligands is first established as a baseline. This baseline is then compared to the change in conformation in going from the apo to holo states to probe induced flexibility. The inherent backbone flexibility across the apo structures is roughly the same as the variation across holo structures. The induced backbone flexibility across apo-holo pairs is larger than that of the apo or holo states, but the increa

SUBMITTER: Clark JJ 

PROVIDER: S-EPMC6370239 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature