Crystal structure of the repetitive segments of spectrin.
Crystal structure of the repetitive segments of spectrin.
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DOI：
10.1126/science.8266097
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发表时间：
1993-12
期刊：
影响因子：
56.9
通讯作者：
Y. Yan;E. Winograd;A. Viel;T. Cronin;S. Harrison;D. Branton
中科院分区：
文献类型：
--
作者：
Y. Yan;E. Winograd;A. Viel;T. Cronin;S. Harrison;D. Branton
血影蛋白家族的细长蛋白(抗肌营养不良蛋白、α-肌动蛋白和血影蛋白)含有重复的片段，并通过交联肌动蛋白细丝形成有弹性的细胞网络。以1.8埃的分辨率测定了α-血影蛋白的一个重复片段的结构。一段由三股螺旋束组成。两个串联节段之间的界面模型表明，节段之间的疏水相互作用可能限制节段间的灵活性。螺旋侧链相互作用解释了已知的导致溶血性贫血的突变是如何破坏维持红细胞膜完整性的血影蛋白结合的。
The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.