Structural coupling between FKBP12 and buried water.

@article{Szp2009StructuralCB,
  title={Structural coupling between FKBP12 and buried water.},
  author={Szilvia Sz{\'e}p and Sheldon Park and Eric T. Boder and Gregory D Van Duyne and Jeffery G. Saven},
  journal={Proteins},
  year={2009},
  volume={74 3},
  pages={603-11}
}
Globular proteins often contain structurally well-resolved internal water molecules. Previously, we reported results from a molecular dynamics study that suggested that buried water (Wat3) may play a role in modulating the structure of the FK506 binding protein-12 (FKBP12) (Park and Saven, Proteins 2005; 60:450-463). In particular, simulations suggested that disrupting a hydrogen bond to Wat3 by mutating E60 to either A or Q would cause a structural perturbation involving the distant W59 side… CONTINUE READING

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