The spectrin repeat folds into a three‐helix bundle in solution

FEBS Letters

Rivas, German²  Pascual, Jaime¹  Pastore, Annalisa¹  Saraste, Matti¹  Pfuhl, Mark¹ 

[1] European Molecular Biology Laboratory, Meyerhofstr. 1, Postfach 102209, D-69012 Heidelberg, Germany;Centro de Investigaciones Biologicas, CSIC, Velazquez 144, 28006 Madrid, Spain

关键词: Spectrin repeat;    Three-helix bundle;    Heteronuclear NMR;    Membrane skeleton;    R16;    16-th repeat of chicken brain α-spectrin;    NOE;    nuclear Overhauser effect;    2D and 3D;    two-and three-dimensional;    respectively;    NOESY;    NOE spectroscopy;    TOCSY;    total correlation spectroscopy;    TOWNY;    TOCSY without NOESY;    TSP;    3-(trimethylsilyl)propionate;    T 1;    longitudinal relaxation time;    T 2;    transverse relaxation time;   

DOI  :  10.1016/0014-5793(96)00251-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Spectrin, a major component of the membrane skeleton, is mainly composed of tandemly repeated segments of approx. 106 amino acids. We have undertaken the determination of the three-dimensional structure of a chicken brain α-spectrin repeat by heteronuclear multidimensional NMR. Sedimentation equilibrium demonstrates that this repeat is monomeric at the concentration used for NMR (1 mM). Its secondary structure was identified using a collection of sequential and medium range NOEs, chemical shifts, HN-Hα coupling constants, and relaxation measurements. These data unequivocally demonstrate the presence of three long helices connected by two loops. A set of interhelical NOEs indicates that the helices assemble into a triple helical structure. Our results provide experimental evidence supporting the triple-helical bundle proposed by modelling.

【 授权许可】

Unknown