Leptin is a four-helix bundle: secondary structure by NMR.
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.
Kline
A D
AD
Lilly Research Laboratories, Lilly Corporate Center, Indianapolis, IN 48285-0403, USA. a.kline@lilly.com
Becker
G W
GW
Churgay
L M
LM
Landen
B E
BE
Martin
D K
DK
Muth
W L
WL
Rathnachalam
R
R
Richardson
J M
JM
Schoner
B
B
Ulmer
M
M
Hale
J E
JE
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D016207:Cytokines / Q000737:chemistry / Q000145:classification; D020738:Leptin; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000145:classification
D002247:Carbon Isotopes; D016207:Cytokines; D020738:Leptin; D009587:Nitrogen Isotopes; D011506:Proteins