Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state.

ABSTRACT: Protein-protein binding usually involves structural changes that may extend beyond the rearrangements on a local scale, and cannot be explained by a classical lock-and-key mechanism. Several models have been advanced to explain the flexible binding of proteins such as the induced fit mechanism where the ligand is postulated to induce a conformational change at the interaction site upon binding, or the preexisting equilibrium hypothesis that assumes that protein samples an ensemble of conformations at equilibrium conditions and that the ligand binds selectively to an active conformation. We explored the equilibrium motions of proteins that exhibit relatively large (nonlocal) conformational changes upon protein binding using the Gaussian network model and the anisotropic network model of pro

SUBMITTER: Tobi D 

PROVIDER: S-EPMC1323175 | biostudies-literature | 2005 Dec

REPOSITORIES: biostudies-literature