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Three-dimensional structure of interleukin 8 in solution.

Clore GM, Appella E, Yamada M, Matsushima K, Gronenborn AM
Biochemistry 29 1689-96 (1990)
Cited: 247 times
EuropePMC logo PMID: 2184886

Abstract

The solution structure of the interleukin 8 (IL-8) dimer has been solved by nuclear magnetic resonance (NMR) spectroscopy and hybrid distance geometry-dynamical simulated annealing calculations. The structure determination is based on a total of 1880 experimental distance restraints (of which 82 are intersubunit) and 362 torsion angle restraints (comprising phi, psi, and chi 1 torsion angles). A total of 30 simulated annealing structures were calculated, and the atomic rms distribution about the mean coordinate positions (excluding residues 1-5 of each subunit) is 0.41 +/- 0.08 A for the backbone atoms and 0.90 +/- 0.08 A for all atoms. The three-dimensional solution structure of the IL-8 dimer reveals a structural motif in which two symmetry-related antiparallel alpha-helices, approximately 24 A long and separated by about 14 A, lie on top of a six-stranded antiparallel beta-sheet platform derived from two three-stranded Greek keys, one from each monomer unit. The general architecture is similar to that of the alpha 1/alpha 2 domains of the human class I histocompatibility antigen HLA-A2. It is suggested that the two alpha-helices form the binding site for the cellular receptor and that the specificity of IL-8, as well as that of a number of related proteins involved in cell-specific chemotaxis, mediation of cell growth, and the inflammatory response, is achieved by the distinct distribution of charged and polar residues at the surface of the helices.

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  2. The marriage of chemokines and galectins as functional heterodimers. von Hundelshausen P, Wichapong K, Gabius HJ, Mayo KH. Cell Mol Life Sci 78 8073-8095 (2021)

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  3. New Insight into Drugs to Alleviate Atopic March via Network Pharmacology-Based Analysis. Oh KK, Adnan M, Cho DH. Curr Issues Mol Biol 44 2257-2274 (2022)


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