Leptin is a four-helix bundle: Secondary structure by NMR

被引：41

作者：

Kline, AD

Becker, GW

Churgay, LM

Landen, BE

Martin, DK

Muth, WL

Rathnachalam, R

Richardson, JM

Schoner, B

Ulmer, M

Hale, JE

机构：

[1] Lilly Research Laboratories, Lilly Corporate Center, Indianapolis

来源：

FEBS LETTERS | 1997年 / 407卷 / 02期

关键词：

nuclear magnetic resonance; leptin; obesity; secondary structure; cytokine-fold;

D O I：

10.1016/S0014-5793(97)00353-0

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：

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.

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页码：239 / 242

页数：4

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