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J. Biol. Chem., Vol. 264, Issue 29, 17595-17605, Oct, 1989
MJ Eck and SR Sprang
The three-dimensional structure of tumor necrosis factor (TNF-alpha), a
protein hormone secreted by macrophages, has been determined at 2.6 A
resolution by x-ray crystallography. Phases were determined by multiple
isomorphous replacement using data collected from five heavy atom
derivatives. The multiple isomorphous replacement phases were further
improved by real space symmetry averaging, exploiting the
noncrystallographic 3-fold symmetry of the TNF-alpha trimer. An atomic
model corresponding to the known amino acid sequence of TNF-alpha was
readily built into the electron density map calculated with these improved
phases. The 17,350-dalton monomer forms an elongated, antiparallel
beta-pleated sheet sandwich with a "jelly-roll" topology. Three monomers
associate intimately about a 3-fold axis of symmetry to form a compact
bell-shaped trimer. Examination of the model and comparison to known
protein structures reveals striking structural homology to several viral
coat proteins, particularly satellite tobacco necrosis virus. Locations of
residues conserved between TNF-alpha and lymphotoxin (TNF-beta, a related
cytokine known to bind to the same receptors as TNF-alpha) suggest that
lymphotoxin, like TNF-alpha, binds to the receptor as a trimer and that the
general site of interaction with the receptor is at the "base" of the
trimer.
The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 95235-9050.
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