Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein

FEBS Letters

Van Eldik, Linda J.²  Kilby, Peter M.¹  Roberts, Gordon C.K.¹ 

[1] Department of Biochemistry and Biological NMR Centre, Adrian Building, University of Leicester, Leicester LE1 7RH, UK;Northwestern University Medical School, Department of Cell and Molecular Biology and Institute for Neuroscience, 303 East Chicago Ave., Chicago, IL 60611-3008, USA

关键词: S100;    Calcium-binding protein;    Nuclear magnetic resonance;    Secondary structure;    S-100;   

DOI  :  10.1016/0014-5793(95)00296-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

S100β 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 S100β. 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 α-helix in S100β.

【 授权许可】

Unknown