Leptin is a four-helix bundle: Secondary structure by NMR
Leptin is a four-helix bundle: Secondary structure by NMR
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DOI：
10.1016/s0014-5793(97)00353-0
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发表时间：
1997-04-28
期刊：
影响因子：
3.5
通讯作者：
Hale, JE
中科院分区：
文献类型：
--
作者：
Kline, AD;Becker, GW;Hale, JE
瘦素是一种信号蛋白，其突变体与肥胖和 II 型糖尿病有关。由于缺乏序列相似性，无法基于与已知系统的结构相似性进行类比。小鼠瘦素（C-13/N-15 标记）的主链 NMR 信号已被确定，其二级结构表明它是一种四螺旋束细胞因子。螺旋长度和二硫键模式与瘦素作为短螺旋细胞因子家族的成员一致。建立了三维模型，验证所识别元素与短螺旋细胞因子核心的机械一致性。 (C) 1997 年欧洲生化学会联合会。
Leptin is a signaling protein that in its mutant has been associated with obesity and Type II diabetes. The lack of sequence similarity has precluded analogies based on structural resemblance to known systems. Backbone NMR signals for mouse leptin (C-13/N-15-labeled) have been assigned and its secondary structure reveals it to be a four-helix bundle cytokine. Helix lengths and disulfide pattern are in agreement with leptin as a member of the short-helix cytokine family. A three-dimensional model was built verifying the mechanical consistency of the identified elements with a short-helix cytokine core. (C) 1997 Federation of European Biochemical Societies.