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FEBS Lett. 1993 Oct 25;333(1-2):123-6.

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

Author information

1
Department of Zoological Cell Biology, Stockholm University, Sweden.

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.

PMID:
8224149
DOI:
10.1016/0014-5793(93)80388-b
[Indexed for MEDLINE]
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