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Mutagenesis of human profilin locates its poly( l ‐prolme)‐bindmg site to a hydrophobic patch of aromatic amino acids
Author(s) -
Björkegren Camilla,
Rozycki Mike,
Schutt Clarence E.,
Lindberg Uno,
Karlsson Roger
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80388-b
Subject(s) - profilin , amino acid , sh3 domain , binding site , chemistry , mutagenesis , homology (biology) , biochemistry , actin , site directed mutagenesis , stereochemistry , actin cytoskeleton , proto oncogene tyrosine protein kinase src , cytoskeleton , mutation , mutant , phosphorylation , gene , cell
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.