Determination of the Monomer-Dimer Equilibrium of Interleukin-8 Reveals It Is a Monomer at Physiological Concentrations

Stephen D. Burrows; Michael L. Doyle; Kenneth P. Murphy; Samuel G. Franklin; John R. White; Ian Brooks; Dean E. McNulty; Miller O. Scott; Jay R. Knutson; Denise Porter; Peter R. Young; Preston Hensley

doi:10.1021/bi00209a002

Determination of the Monomer-Dimer Equilibrium of Interleukin-8 Reveals It Is a Monomer at Physiological Concentrations

Stephen D. Burrows, Michael L. Doyle, Kenneth P. Murphy, Samuel G. Franklin, John R. White, Ian Brooks, Dean E. McNulty, Miller O. Scott, Jay R. Knutson, Denise Porter, Peter R. Young, Preston Hensley

Research output: Contribution to journal › Article › peer-review

Abstract

Interleukin-8 has been shown by X-ray crystallography and NMR to be a homodimer, suggesting that this is the form which binds to its receptor. Here we measure, for the first time, the monomer-dimer equilibrium of interleukin-8 using analytical ultracentrifugation and titration microcalorimetry and find that it dissociates readily to monomers with an equilibrium dissociation constant of 18 ± 6 μ at 37 °C. The present findings suggest that the monomer is the form which binds to the receptor. Comparison of experimental and structure-based calculated thermodynamics of interleukin-8 dimerization argues for limited subunit conformational changes upon dissociation to monomer.

Original language	English (US)
Pages (from-to)	12741-12745
Number of pages	5
Journal	Biochemistry
Volume	33
Issue number	43
DOIs	https://doi.org/10.1021/bi00209a002
State	Published - Nov 1 1994
Externally published	Yes

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Biochemistry

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10.1021/bi00209a002

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Burrows, S. D., Doyle, M. L., Murphy, K. P., Franklin, S. G., White, J. R., Brooks, I., McNulty, D. E., Scott, M. O., Knutson, J. R., Porter, D., Young, P. R., & Hensley, P. (1994). Determination of the Monomer-Dimer Equilibrium of Interleukin-8 Reveals It Is a Monomer at Physiological Concentrations. Biochemistry, 33(43), 12741-12745. https://doi.org/10.1021/bi00209a002

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abstract = "Interleukin-8 has been shown by X-ray crystallography and NMR to be a homodimer, suggesting that this is the form which binds to its receptor. Here we measure, for the first time, the monomer-dimer equilibrium of interleukin-8 using analytical ultracentrifugation and titration microcalorimetry and find that it dissociates readily to monomers with an equilibrium dissociation constant of 18 ± 6 μ at 37 °C. The present findings suggest that the monomer is the form which binds to the receptor. Comparison of experimental and structure-based calculated thermodynamics of interleukin-8 dimerization argues for limited subunit conformational changes upon dissociation to monomer.",

author = "Burrows, {Stephen D.} and Doyle, {Michael L.} and Murphy, {Kenneth P.} and Franklin, {Samuel G.} and White, {John R.} and Ian Brooks and McNulty, {Dean E.} and Scott, {Miller O.} and Knutson, {Jay R.} and Denise Porter and Young, {Peter R.} and Preston Hensley",

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T1 - Determination of the Monomer-Dimer Equilibrium of Interleukin-8 Reveals It Is a Monomer at Physiological Concentrations

AU - Burrows, Stephen D.

AU - Doyle, Michael L.

AU - Murphy, Kenneth P.

AU - Franklin, Samuel G.

AU - White, John R.

AU - Brooks, Ian

AU - McNulty, Dean E.

AU - Scott, Miller O.

AU - Knutson, Jay R.

AU - Porter, Denise

AU - Young, Peter R.

AU - Hensley, Preston

PY - 1994/11/1

Y1 - 1994/11/1

N2 - Interleukin-8 has been shown by X-ray crystallography and NMR to be a homodimer, suggesting that this is the form which binds to its receptor. Here we measure, for the first time, the monomer-dimer equilibrium of interleukin-8 using analytical ultracentrifugation and titration microcalorimetry and find that it dissociates readily to monomers with an equilibrium dissociation constant of 18 ± 6 μ at 37 °C. The present findings suggest that the monomer is the form which binds to the receptor. Comparison of experimental and structure-based calculated thermodynamics of interleukin-8 dimerization argues for limited subunit conformational changes upon dissociation to monomer.

AB - Interleukin-8 has been shown by X-ray crystallography and NMR to be a homodimer, suggesting that this is the form which binds to its receptor. Here we measure, for the first time, the monomer-dimer equilibrium of interleukin-8 using analytical ultracentrifugation and titration microcalorimetry and find that it dissociates readily to monomers with an equilibrium dissociation constant of 18 ± 6 μ at 37 °C. The present findings suggest that the monomer is the form which binds to the receptor. Comparison of experimental and structure-based calculated thermodynamics of interleukin-8 dimerization argues for limited subunit conformational changes upon dissociation to monomer.

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Determination of the Monomer-Dimer Equilibrium of Interleukin-8 Reveals It Is a Monomer at Physiological Concentrations

Abstract

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