CRYSTAL-STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN

被引：329

作者：

YAN, Y

WINOGRAD, E

VIEL, A

CRONIN, T

HARRISON, SC

BRANTON, D

机构：

[1] HARVARD UNIV,HOWARD HUGHES MED INST,CAMBRIDGE,MA 02138

[2] HARVARD UNIV,DEPT CELLULAR & DEV BIOL,CAMBRIDGE,MA 02138

来源：

SCIENCE | 1993年 / 262卷 / 5142期

关键词：

D O I：

10.1126/science.8266097

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

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页码：2027 / 2030

页数：4

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