Determination of the Secondary Structure and Folding Topology of Human Interleukin-4 Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy

Robert Powers, Daniel S. Garrett, Carl J. March, Eric A. Frieden, Angela M. Gronenbom, G. Marius Clore

Research output: Contribution to journalArticle

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Abstract

The secondary structure of human recombinant interleukin-4 (IL-4) has been investigated by three-dimensional (3D) 15N- and 13C-edited nuclear Overhauser (NOE) spectroscopy on the basis of the 1H, 15N, and 13C assignments presented in the preceding paper [Powers, R., Garrett, D. S., March, C. J., Frieden, E. A., Gronenborn, A. M., ' Clore, G. M., (1992) Biochemistry (preceding paper in this issue)]. Based on the NOE data involving the NH, CαH, and CβH protons, as well as 3JHnα coupling constant, amide exchange, and 13Cα and 13Cβ secondary chemical shift data, it is shown that IL-4 consists offour long helices (residues 9-21, 45-64, 74-96, and 113-129), two small helical turns (residues 27-29 and 67-70), and a mini antiparallel β-sheet (residues 32-34 and 110-112). In addition, the topological arrangement of the helices and the global fold could be readily deduced from a number oflong-range interhelical NOEs identified in the 3D 13C-edited NOE spectrum in combination with the spatial restrictions imposed by three disulfide bridges. These data indicate that the helices ofinterleukin-4 are arranged in a left-handed four-helix bundle with two overhand connections.

Original languageEnglish (US)
Pages (from-to)4347-4353
Number of pages7
JournalBiochemistry
Volume31
Issue number17
DOIs
StatePublished - Jan 1 1992

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Magnetic resonance spectroscopy
Interleukin-4
Magnetic Resonance Spectroscopy
Topology
Biochemistry
Chemical shift
Amides
Disulfides
Protons
Spectrum Analysis
Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

Determination of the Secondary Structure and Folding Topology of Human Interleukin-4 Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy. / Powers, Robert; Garrett, Daniel S.; March, Carl J.; Frieden, Eric A.; Gronenbom, Angela M.; Clore, G. Marius.

In: Biochemistry, Vol. 31, No. 17, 01.01.1992, p. 4347-4353.

Research output: Contribution to journalArticle

Powers, Robert ; Garrett, Daniel S. ; March, Carl J. ; Frieden, Eric A. ; Gronenbom, Angela M. ; Clore, G. Marius. / Determination of the Secondary Structure and Folding Topology of Human Interleukin-4 Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy. In: Biochemistry. 1992 ; Vol. 31, No. 17. pp. 4347-4353.
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abstract = "The secondary structure of human recombinant interleukin-4 (IL-4) has been investigated by three-dimensional (3D) 15N- and 13C-edited nuclear Overhauser (NOE) spectroscopy on the basis of the 1H, 15N, and 13C assignments presented in the preceding paper [Powers, R., Garrett, D. S., March, C. J., Frieden, E. A., Gronenborn, A. M., ' Clore, G. M., (1992) Biochemistry (preceding paper in this issue)]. Based on the NOE data involving the NH, CαH, and CβH protons, as well as 3JHnα coupling constant, amide exchange, and 13Cα and 13Cβ secondary chemical shift data, it is shown that IL-4 consists offour long helices (residues 9-21, 45-64, 74-96, and 113-129), two small helical turns (residues 27-29 and 67-70), and a mini antiparallel β-sheet (residues 32-34 and 110-112). In addition, the topological arrangement of the helices and the global fold could be readily deduced from a number oflong-range interhelical NOEs identified in the 3D 13C-edited NOE spectrum in combination with the spatial restrictions imposed by three disulfide bridges. These data indicate that the helices ofinterleukin-4 are arranged in a left-handed four-helix bundle with two overhand connections.",
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