NMR structure of the WIF domain of the human Wnt-inhibitory factor-1.

@article{Liepinsh2006NMRSO,
  title={NMR structure of the WIF domain of the human Wnt-inhibitory factor-1.},
  author={Edvards Liepinsh and L{\'a}szl{\'o} B{\'a}nyai and L{\'a}szl{\'o} Patthy and Gottfried Otting},
  journal={Journal of molecular biology},
  year={2006},
  volume={357 3},
  pages={942-50}
}
The human Wnt-binding protein Wnt-inhibitory factor-1 (WIF-1) comprises an N-terminal WIF module followed by five EGF-like repeats. Here we report the three-dimensional structure of the WIF domain of WIF-1 determined by NMR spectroscopy. The fold consists of an eight-stranded beta-sandwich reminiscent of the immunoglobulin fold. Residual detergent (Brij-35) used in the refolding protocol was found to bind tightly to the WIF domain. The binding site was identified by intermolecular nuclear… CONTINUE READING