The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition
The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition
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DOI：
10.1021/bi060717k
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发表时间：
2006-10-31
期刊：
影响因子：
2.9
通讯作者：
Laue, Ernest D.
中科院分区：
文献类型：
--
作者：
Casal, Eva;Federici, Luca;Laue, Ernest D.
BAR结构域存在于结合和重塑膜并参与细胞骨架和核过程的蛋白质中。在这里，我们报告的晶体结构的BAR域从人类Bin 1蛋白在2.0埃分辨率。同源二聚体Bin 1BAR结构域的四级和三级结构都是建立在侧链的“钮入孔”包装上的，就像在传统的左手卷曲螺旋中发现的那些，并且这种包装控制了推定的膜接合凹面的曲率。我们的计算表明，Bin 1BAR域包含两个潜在的网站上的二聚体的凸面蛋白质-蛋白质相互作用。结构特征的比较分析显示，至少有三种结构亚型的BAR结构域编码在人类基因组中，由Arfaptin，Bin 1/Amphiphysin，和IRSp 53 BAR结构域。我们将讨论这些主要群体如何在形成调控异型相互作用的潜力方面有所不同。
BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 angstrom resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon "knobs-into-holes" packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein-protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups may differ in their potential to form regulatory heterotypic interactions.