Critical residue that promotes protein dimerization: a story of partially exposed Phe25 in 14-3-3σ.

ABSTRACT: Many proteins exist and function as oligomers. While hydrophobic interactions have been recognized as the major driving force for oligomerization, detailed molecular mechanisms for the assembly are unknown. Here, we used 14-3-3σ as a model protein and investigated the role of hydrophobic residues at the dimeric interface using MD simulations and coimmunoprecipitations. We found that a half-exposed and half-buried residue in the interface, Phe(25), plays a more important role in promoting homodimerization than the hydrophobic core residues by organizing both favorable hydrophobic and hydrophilic interactions. Phe(25) is critical in packing and stabilizing hydrophobic core residues. We conclude that the structural stability of hydrophobic cores is critical for a stable homodimer complex and

SUBMITTER: Liu JY 

PROVIDER: S-EPMC3322420 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature