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 S Brooks, Dean E. McNulty, Miller O. Scott, Jay R. Knutson, Denise Porter, Peter R. Young, Preston Hensley

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)12741-12745
Number of pages5
JournalBiochemistry
Volume33
Issue number43
DOIs
StatePublished - Nov 1 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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    Burrows, S. D., Doyle, M. L., Murphy, K. P., Franklin, S. G., White, J. R., Brooks, I. S., 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