Profilin binds proline-rich ligands in two distinct amide backbone orientations
Profilin binds proline-rich ligands in two distinct amide backbone orientations
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DOI：
10.1038/10722
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发表时间：
1999-07-01
期刊：
影响因子：
--
通讯作者：
Almo, SC
中科院分区：
文献类型：
--
作者：
Mahoney, NM;Rozwarski, DA;Almo, SC
肌动蛋白调节蛋白profilin通过与嵌入其结合伴侣中的高度富含脯氨酸的基序相互作用而靶向特定的细胞区域。新的X射线晶体学结果表明，profilin，像SH3域，可以结合脯氨酸丰富的配体在两个不同的酰胺骨架方向。通过与SH3结构域的进一步类比，这些数据表明，profilin配体中的非脯氨酸残基可能决定结合的极性和寄存器，以及涉及profilin的组装体的详细组织。这种简并性可能是结合富含脯氨酸的配体（包括WW和EVH1结构域）的模块的一般特征，并且对参与肌动蛋白细胞骨架的信号传导和调节的大分子复合物的组装和活性具有影响。
actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly proline-rich motifs embedded within its binding partners. New X-ray crystallographic results demonstrate that profilin, like SH3 domains, can bind proline-rich ligands in two distinct amide backbone orientations. By further analogy with SH3 domains, these data suggest that non-proline residues in profilin ligands may dictate the polarity and register of binding, and the detailed organization of the assemblies involving profilin. This degeneracy may be a general feature of modules that bind proline-rich ligands, including WW and EVH1 domains, and has implications for the assembly and activity of macromolecular complexes involved in signaling and the regulation of the actin cytoskeleton.