Leptin is a four‐helix bundle: secondary structure by NMR

FEBS Letters

Becker, Gerald W¹  Richardson, John M¹  Churgay, Lisa M¹  Landen, Bryan E¹  Martin, Debra K¹  Rathnachalam, Radhakrishnan¹  Kline, Allen D¹  Schoner, Brigitte¹  Hale, John E¹  Muth, William L¹  Ulmer, Maverick¹ 

[1] Lilly Research Laboratories, Lilly Corporate Center, Indianapolis, IN 48285-0403, USA

关键词: Nuclear magnetic resonance;    Leptin;    Obesity;    Secondary structure;    Cytokine-fold;    CD;    circular dichroism;    CSI;    chemical shift index;    IL-6;    interleukin-6;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;   

DOI  :  10.1016/S0014-5793(97)00353-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Leptin is a signaling protein that in its mutant forms 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 (¹³C/¹⁵N -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.

【 授权许可】

Unknown