| Literature DB >> 7947677 |
S D Burrows1, M L Doyle, K P Murphy, S G Franklin, J R White, I Brooks, D E McNulty, M O Scott, J R Knutson, D Porter.
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 microM at 37 degrees 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.Entities:
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Year: 1994 PMID： 7947677 DOI： 10.1021/bi00209a002
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162