The leptin haemopoietic cytokine fold is stabilized by an intrachain disulfide bond

Hormone and Metabolic Research

Volumn 28, Issue 12, 1996, Pages 649-652

  Rock, F L ^a   Altmann, S W ^a   Van Heek, M ^a   Kastelein, R A ^a   Bazan, J F ^a  

^a MERCK RESEARCH LABORATORIES   (United States)

Author keywords

circular dichroism; cytokine superfamily; leptin; structure function analysis

Indexed keywords

LEPTIN;

ANIMAL EXPERIMENT; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISULFIDE BOND; FOOD INTAKE; HUMAN; MOLECULAR DYNAMICS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN VARIANT;

EID: 0030455390     PISSN: 00185043     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-979871     Document Type: Article

References (14)

1. Zhang Y, Proenca R, Maffei M, Barone M, Leopold L, Friedman JM: Positional cloning of the mouse obese gene and its human homologue. Nature 372: 425-432 (1994).
2. Madej T, Boguski MS, Bryant H: Threading analysis suggests that the obese gene product may be a helical cytokine. Febs Lett 373: 13-18 (1995).
3. Bazan JF, Altmann SW, Rock FL, Kastelein RA: Molecular modeling and biophysical analysis of the helical cytokine fold (submitted).
4. Tartaglia LA, Dembski M, Weng X, Deng N, Culpepper J, Devos R, Richards GJ, Campfield LA, Clark FT, Deeds J: Identification and expression cloning of a leptin receptor, OB-R. Cell 83: 1263-1271 (1996).
5. Altmann SW, Timans JC, Rock FL, Bazan JF, Kastelein RA: Expression and purification of a synthetic human obese gene product. Protein Expression and Purification 6: 722-726 (1995).
6. Rock FL, Li X, Chong P, Ida N, Klein M: Roles of disulfide bonds in recombinant human interleukin 6 conformation. Biochemistry 33: 5146-5154 (1994).
7. Sreerama N, Woody RW: A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209: 32-44 (1993).
8. Sprang SR, Bazan JF: Cytokine structural taxonomy and mechanisms of receptor engagement. Current Opinion in Structural Biology 5: 114-121 (1993).
9. Wells JA, de Vos AM: Structure and function of human growth hormone: implications for the hematopoietins. Annu Rev Biophys Biomol Struct 22: 329-351 (1993).
10. Pelleymounter MA, Cullen MJ, Baker MB, Hecht R, Winters D, Boone T, Collins F: Effects of the obese gene product on body weight regulation in ob/ob mice. Science 269: 540-543 (1995).
11. Halaas JL, Gajiwala KS, Maffei M, Cohen SL, Chait BT, Rabinowitz D, Lallone RL, Burley SK, Friedman JM: Weight-reducing effects of the plasma protein encoded by the obese gene. Science 269: 543-546 (1995).
12. Campfield LA, Smith FJ, Cuisez Y, Devos R, Burn P: Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks. Science 269: 546-549 (1995).
13. Windsor WT, Syto R, Le HV, Trotta PP: Analysis of the conformation and stability of Escherichia coli derived recombinant human interleukin 4 by circular dichroism. Biochemistry 30: 1259-1264 (1991)
14. Wingfield P, Graber P, Moonen P, Craig S, Pain RH: The conformation and stability of recombinant-derived granulocyte-macrophage colony stimulating factors. Eur J Biochem 173: 65-72 (1988).