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.
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页码：90 / 96
页数：7
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