Leptin is a four-helix bundle: secondary structure by NMR
| Autor: | Debra K Martin, John M. Richardson, Gerald W. Becker, John E. Hale, Radhakrishnan Rathnachalam, Lisa M. Churgay, Muth William Lawrence, Maverick Ulmer, Allen D Kline, Bryan E. Landen, Brigitte Elisabeth Schoner |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Leptin medicine.medical_specialty Circular dichroism Magnetic Resonance Spectroscopy Molecular Sequence Data Biophysics Biochemistry Protein Structure Secondary Chemical shift index Nuclear magnetic resonance Mice Structural Biology Internal medicine Secondary structure Genetics medicine Animals Amino Acid Sequence Obesity Molecular Biology Peptide sequence Protein secondary structure Helix bundle Carbon Isotopes Nitrogen Isotopes Chemistry Proteins Cell Biology Nuclear magnetic resonance spectroscopy Cell biology Endocrinology Helix Cytokines Cytokine-fold |
| Zdroj: | FEBS Letters. (2):239-242 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(97)00353-0 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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