NUCLEAR-MAGNETIC-RESONANCE ASSIGNMENTS AND SECONDARY STRUCTURE OF BOVINE S100-BETA PROTEIN

被引：12

作者：

KILBY, PM

VANELDIK, LJ

ROBERTS, GCK

机构：

[1] UNIV LEICESTER,BIOL NMR CTR,LEICESTER LE1 7RH,LEICS,ENGLAND

[2] NORTHWESTERN UNIV,SCH MED,DEPT MOLEC & CELL BIOL,CHICAGO,IL 60611

[3] INST NEUROSCI,CHICAGO,IL 60611

来源：

FEBS LETTERS | 1995年 / 363卷 / 1-2期

基金：

英国惠康基金;

关键词：

S100; CALCIUM-BINDING PROTEIN; NUCLEAR MAGNETIC RESONANCE; SECONDARY STRUCTURE; S-100;

D O I：

10.1016/0014-5793(95)00296-L

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

S100 beta is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D-9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100 beta. The secondary structure is similar to that of calbindin D-9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue alpha-helix in S100 beta.

引用

页码：90 / 96

页数：7

共 23 条

[1] 3-DIMENSIONAL SOLUTION STRUCTURE OF CA2+-LOADED PORCINE CALBINDIN-D9K DETERMINED BY NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY [J].