Mutagenesis of human profilin locates its poly(L-proline)-binding site to a hydrophobic patch of aromatic amino acids.

@article{Bjrkegren1993MutagenesisOH,
  title={Mutagenesis of human profilin locates its poly(L-proline)-binding site to a hydrophobic patch of aromatic amino acids.},
  author={C Bj{\"o}rkegren and Michael D. Rozycki and Clarence Schutt and Uno Lindberg and Roger Karlsson},
  journal={FEBS letters},
  year={1993},
  volume={333 1-2},
  pages={123-6}
}
The actin-binding protein, profilin, contains a src-homology (SH) 3-like fold (Schutt, C.E. et al., submitted), and its tight interaction with poly(L-proline) is reminiscent of the binding activity exhibited by SH3-domains. Here we demonstrate that replacements of aromatic amino acids in a hydrophobic patch on the surface of the profilin molecule abolish its poly(L-proline)-binding capacity. However, the location of this hydrophobic patch is found in another region of the molecule than that… CONTINUE READING