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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acids / chemistry
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Amino Acids / metabolism
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Binding Sites
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Contractile Proteins*
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Humans
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Microfilament Proteins / chemistry*
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism
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Mutagenesis
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Peptides / metabolism*
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Profilins
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae
Substances
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Amino Acids
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Contractile Proteins
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Microfilament Proteins
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PFN1 protein, human
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Peptides
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Profilins
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Recombinant Proteins
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polyproline