Restricted mobility of conserved residues in protein-protein interfaces in molecular simulations.

ABSTRACT: Conserved residues in protein-protein interfaces correlate with residue hot-spots. To obtain insight into their roles, we have studied their mobility. We have performed 39 explicit solvent simulations of 15 complexes and their monomers, with the interfaces varying in size, shape, and function. The dynamic behavior of conserved residues in unbound monomers illustrates significantly lower flexibility as compared to their environment, suggesting that already before binding they are constrained in a boundlike configuration. To understand this behavior, we have analyzed the inter- and intrachain hydrogen-bond residence-time in the interfaces. We find that conserved residues are not involved significantly in hydrogen bonds across the interface as compared to nonconserved. However, the monomer si

SUBMITTER: Yogurtcu ON 

PROVIDER: S-EPMC2292389 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature