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Leptin is a four‐helix bundle: secondary structure by NMR
Author(s) -
Kline Allen D,
Becker Gerald W,
Churgay Lisa M,
Landen Bryan E,
Martin Debra K,
Muth William L,
Rathnachalam Radhakrishnan,
Richardson John M,
Schoner Brigitte,
Ulmer Maverick,
Hale John E
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00353-0
Subject(s) - helix (gastropod) , leptin , bundle , structural similarity , helix bundle , mutant , cytokine , chemistry , protein secondary structure , protein structure , crystallography , biology , medicine , endocrinology , biochemistry , obesity , materials science , gene , ecology , snail , composite material
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 ( 13 C/ 15 N ‐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.