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

FEBS Lett. 1993 Oct 25;333(1-2):123-6. doi: 10.1016/0014-5793(93)80388-b.

Abstract

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 displaying structural similarities with SH3 domains.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / chemistry
  • Amino Acids / metabolism
  • Binding Sites
  • Contractile Proteins*
  • Humans
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • Mutagenesis
  • Peptides / metabolism*
  • Profilins
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae

Substances

  • Amino Acids
  • Contractile Proteins
  • Microfilament Proteins
  • PFN1 protein, human
  • Peptides
  • Profilins
  • Recombinant Proteins
  • polyproline