Structures of the spectrin-ankyrin interaction binding domains
Structures of the spectrin-ankyrin interaction binding domains
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DOI：
10.1182/blood-2008-10-184358
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发表时间：
2009-05-28
期刊：
影响因子：
20.3
通讯作者：
Mondragon, Alfonso
中科院分区：
文献类型：
--
作者：
Ipsaro, Jonathan J.;Huang, Lei;Mondragon, Alfonso
作为红细胞膜骨架的关键成分，spectrin和锚蛋白特异性地相互作用，将spectrin细胞骨架系在细胞膜上。求解了锚蛋白的谱蛋白结合域和谱蛋白的锚蛋白结合域的结构，阐明了锚蛋白-谱蛋白识别的结构基础。spectrin重复序列14和15的结构表明，这些重复序列与所有其他spectrin重复序列相似。一个可以解释锚蛋白对这些重复序列的偏好的特征是，在重复序列14的一侧存在一个保守的带负电荷的补丁。锚蛋白ZU5结构域的结构显示了一个包含β核的新结构。该结构揭示了规范的ZU5共识序列可能缺少一个重要的区域，该区域编码形成该结构域核心部分的β链。此外，带正电的区域暗示了带负电的谱图重复14的结合面。先前报道的锚蛋白突变大部分位于蛋白质的表面，尽管至少有一个可能是核心的一部分。（血液。2009;113:5385-5393）
As key components of the erythrocyte membrane skeleton, spectrin and ankyrin specifically interact to tether the spectrin cytoskeleton to the cell membrane. The structure of the spectrin binding domain of ankyrin and the ankyrin binding domain of spectrin have been solved to elucidate the structural basis for ankyrin-spectrin recognition. The structure of repeats 14 and 15 of spectrin shows that these repeats are similar to all other spectrin repeats. One feature that could account for the preference of ankyrin for these repeats is the presence of a conserved, negatively charged patch on one side of repeat 14. The structure of the ankyrin ZU5 domain shows a novel structure containing a beta core. The structure reveals that the canonical ZU5 consensus sequence is likely to be missing an important region that codes for a beta strand that forms part of the core of the domain. In addition, a positively charged region is suggestive of a binding surface for the negatively charged spectrin repeat 14. Previously reported mutants of ankyrin that map to this region lie mostly on the surface of the protein, although at least one is likely to be part of the core. (Blood. 2009; 113: 5385-5393)