Björkegren C, Rozycki M, Schutt C E, Lindberg U, Karlsson R
Department of Zoological Cell Biology, Stockholm University, Sweden.
FEBS Lett. 1993 Oct 25;333(1-2):123-6. doi: 10.1016/0014-5793(93)80388-b.
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.
肌动蛋白结合蛋白——原肌球蛋白，含有一个类src同源（SH）3结构域（舒特，C.E.等人，已投稿），并且它与聚（L-脯氨酸）的紧密相互作用让人联想到SH3结构域所表现出的结合活性。在此我们证明，原肌球蛋白分子表面疏水区域中芳香族氨基酸的替换会消除其与聚（L-脯氨酸）的结合能力。然而，该疏水区域的位置位于分子的另一个区域，而非与SH3结构域具有结构相似性的区域。
