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

FEBS Lett. 1997 Apr 28;407(2):239-42. doi: 10.1016/s0014-5793(97)00353-0.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbon Isotopes
  • Cytokines / chemistry
  • Cytokines / classification
  • Leptin
  • Magnetic Resonance Spectroscopy
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Nitrogen Isotopes
  • Protein Structure, Secondary*
  • Proteins / chemistry*
  • Proteins / classification

Substances

  • Carbon Isotopes
  • Cytokines
  • Leptin
  • Nitrogen Isotopes
  • Proteins