1ikm
NMR STUDY OF MONOMERIC HUMAN INTERLEUKIN-8 (30 STRUCTURES)
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OverviewOverview
The solution structure of a monomeric form of interleukin-8 (IL-8) has, been solved using 1H NMR spectroscopy. The chemically synthesized, nonnatural analog [IL-8 (4-72) L25 NH-->NCH3] has the same activity as, that of native IL-8. Thirty structures were generated using the hybrid, distance geometry and simulated annealing protocol using the program, X-PLOR. The structure is well-defined except for N-terminal residues 4-6, and C-terminal residues 67-72. The rms distribution about the average, structure for residues 7-66 is 0.38 A for the backbone atoms and 0.87 A, for all heavy atoms. The structure consists of a series of turns and loops, followed by a triple-stranded beta sheet and a C-terminal alpha helix. The, structure of the monomer is largely similar to the native dimeric IL-8, structures previously determined by both NMR and X-ray methods. The major, difference is that, in the monomeric analog, the C-terminal residues 67-72, are disordered whereas they are helical in the two dimeric structures. The, best fit superposition of the backbone atoms of residues 7-66 of the, monomer structure on the dimeric IL-8 structures showed rms differences of, 1.5 and 1.2 A respectively. The turn (residues 31-35), which is disulfide, linked to the N-terminal region, adopts a conformation in the monomer, similar to that seen in the dimeric X-ray structure (rms difference 1.4 A), and different from that seen in the dimeric NMR structure (rms difference, 2.7 A).(ABSTRACT TRUNCATED AT 250 WORDS)
DiseaseDisease
Known disease associated with this structure: AIDS, slow progression to OMIM:[146929]
About this StructureAbout this Structure
1IKM is a Single protein structure of sequence from Homo sapiens with CH3 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
1H NMR solution structure of an active monomeric interleukin-8., Rajarathnam K, Clark-Lewis I, Sykes BD, Biochemistry. 1995 Oct 10;34(40):12983-90. PMID:7548056
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