MM-PBSA Captures Key Role of Intercalating Water Molecules at a Protein-Protein Interface.

ABSTRACT: The calculation of protein interaction energetics is of fundamental interest, yet accurate quantities are difficult to obtain due to the complex and dynamic nature of protein interfaces. This is further complicated by the presence of water molecules, which can exhibit transient interactions of variable duration and strength with the protein surface. The T-cell receptor (TCR) and its staphylococcal enterotoxin 3 (SEC3) binding partner are well-characterized examples of a protein-protein interaction system exhibiting interfacial plasticity, cooperativity, and additivity among mutants. Specifically engineered mutants induce intercalating interfacial water molecules, which subsequently enhance protein-protein binding affinity. In this work, we perform a set of molecular mechanics (MM) Poisson-

SUBMITTER: Wong S 

PROVIDER: S-EPMC2651627 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature