2il8
From Proteopedia
THREEDIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe solution structure of the interleukin 8 (IL8) dimer has been solved by nuclear magnetic resonance (NMR) spectroscopy and hybrid distance geometrydynamical 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 15 of each subunit) is 0.41 +/ 0.08 A for the backbone atoms and 0.90 +/ 0.08 A for all atoms. The threedimensional solution structure of the IL8 dimer reveals a structural motif in which two symmetryrelated antiparallel alphahelices, approximately 24 A long and separated by about 14 A, lie on top of a sixstranded antiparallel betasheet platform derived from two threestranded 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 HLAA2. It is suggested that the two alphahelices form the binding site for the cellular receptor and that the specificity of IL8, as well as that of a number of related proteins involved in cellspecific 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. Threedimensional structure of interleukin 8 in solution.,Clore GM, Appella E, Yamada M, Matsushima K, Gronenborn AM Biochemistry. 1990 Feb 20;29(7):168996. PMID:2184886^{[1]} From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
