Localization and Structure of the Ankyrin-binding Site on β2-Spectrin
Localization and Structure of the Ankyrin-binding Site on β2-Spectrin
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DOI：
10.1074/jbc.m809245200
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发表时间：
2009-03-13
影响因子：
4.8
通讯作者：
Michaely, Peter
中科院分区：
文献类型：
--
作者：
Davis, Lydia;Abdi, Khadar;Michaely, Peter
血影蛋白是四聚体肌动蛋白交联蛋白，在细胞膜的细胞质表面形成弹性网络，称为膜骨架。在质膜上，膜骨架提供必要的支撑，防止膜材料因环境剪切应力而损失。骨架还控制对细胞和组织功能至关重要的膜蛋白的位置、丰度和活性。骨架调节膜稳定性和功能的能力需要将骨架与膜结合的衔接蛋白。主要的接头是锚蛋白，它与血影蛋白的β亚基和许多整合膜蛋白的细胞质结构域结合。在这里，我们以 1.95 A 分辨率展示了人 β(2)-血影蛋白锚蛋白结合域的晶体结构，以及识别 β(2)-血影蛋白上锚蛋白结合表面的诱变数据。
Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the beta-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human beta(2)-spectrin at 1.95 A resolution together with mutagenesis data identifying the binding surface for ankyrins on beta(2)-spectrin.