Three-dimensional structure of interleukin 8 in solution
- National Institutes of Health, Bethesda, MD (USA)
- National Cancer Institute, Frederick, MD (USA)
- Dainippon Pharmaceutical Company, Osaka (Japan)
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 1,880 experimental distance restraints (of which 82 are intersubunit) and 362 torsion angle restraints (comprising {phi}, {psi}, and {chi}{sub 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 {plus minus} 0.08 {angstrom} for the backbone atoms and 0.90 {plus minus} 0.08 {angstrom} 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 {angstrom} long and separated by about 14 {angstrom}, lie on top of 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.
- OSTI ID:
- 6828854
- Journal Information:
- Biochemistry; (USA), Vol. 29:7; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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550201* - Biochemistry- Tracer Techniques