title: Mutagenesis of human profilin locates its poly(L-proline)-binding site to a hydrophobic patch of aromatic amino acids.
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.
authors.affiliation: Department of Zoological Cell Biology, Stockholm University, Sweden.
authors.forename: C
authors.initials: C
authors.lastname: Björkegren
authors.forename: M
authors.initials: M
authors.lastname: Rozycki
authors.forename: C E
authors.initials: CE
authors.lastname: Schutt
authors.forename: U
authors.initials: U
authors.lastname: Lindberg
authors.forename: R
authors.initials: R
authors.lastname: Karlsson
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D003285:Contractile Proteins; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016296:Mutagenesis; D010455:Peptides / Q000378:metabolism*; D051304:Profilins; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae
chemical_list: D000596:Amino Acids; D003285:Contractile Proteins; D008840:Microfilament Proteins; C495738:PFN1 protein, human; D010455:Peptides; D051304:Profilins; D011994:Recombinant Proteins; C011083:polyproline