血影蛋白重复片段的晶体结构。

Crystal structure of the repetitive segments of spectrin.

作者信息

Yan Y, Winograd E, Viel A, Cronin T, Harrison S C, Branton D

机构信息

Department of Biochemistry, Harvard University, Cambridge, MA 02138.

出版信息

Science. 1993 Dec 24;262(5142):2027-30. doi: 10.1126/science.8266097.

DOI:10.1126/science.8266097

PMID:8266097

Abstract

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.

摘要

血影蛋白家族（肌营养不良蛋白、α-辅肌动蛋白和血影蛋白）的细长蛋白质含有串联重复片段，并通过交联肌动蛋白丝形成有弹性的细胞网络。α-血影蛋白的一个重复片段的结构在1.8埃分辨率下得以确定。一个片段由一个三螺旋束组成。两个串联片段之间界面的模型表明，片段之间的疏水相互作用可能会限制片段间的灵活性。螺旋侧链相互作用解释了已知会导致溶血性贫血的突变如何破坏维持红细胞膜完整性的血影蛋白关联。