2il8
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THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: AIDS, slow progression to OMIM:[146929]
About this StructureAbout this Structure
2IL8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of interleukin 8 in solution., Clore GM, Appella E, Yamada M, Matsushima K, Gronenborn AM, Biochemistry. 1990 Feb 20;29(7):1689-96. PMID:2184886
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