Crystal structure of interleukin 8: symbiosis of NMR and crystallography.
The crystal structure of a host defense system chemotactic factor, interleukin 8, has been solved by molecular replacement using as a model the solution structure derived from nuclear magnetic resonance experiments. The structure was refined with 2 A x-ray data to an R factor of 0.187 (0.217 at 1.6 A). A comparison indicates some potential differences between the structure in solution and in the crystalline state. Our analysis also predicts that residues 4 through 9 on the amino terminus and the beta-bend, which includes His-33, may be important for receptor binding.
Baldwin
E T
ET
Crystallography Laboratory, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.
Weber
I T
IT
St Charles
R
R
Xuan
J C
JC
Appella
E
E
Yamada
M
M
Matsushima
K
K
Edwards
B F
BF
Clore
G M
GM
Gronenborn
A M
AM
D000595:Amino Acid Sequence; D000818:Animals; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D006860:Hydrogen Bonding; D016209:Interleukin-8 / Q000737:chemistry* / Q000302:isolation & purification; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
D016209:Interleukin-8; D011994:Recombinant Proteins