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Activation of the cell surface receptors for tumor necrosis
factor (TNF) is effected by the aggregation of cytoplasmic domains that
occurs when the extracellular domains of two or three receptors bind to
trimeric TNF
Volume 270,
Number 22,
Issue of June 2, pp. 13303-13307, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
or TNF
. The structure of the type I TNF receptor
extracellular domain (sTNF-R1), crystallized in the absence of TNF, has
now been determined at 2.25-Å resolution. The receptor itself is
an elongated molecule comprising four disulfide-rich domains in a
nearly linear array. Contrary to expectations, the unliganded domains
are found to associate into dimers of two distinct types, in which
monomers are related by local two-fold axes of symmetry. In one case,
the receptors are antiparallel to each other and associate through an
interface that overlaps the TNF binding site. If intact receptors were
capable of such an association, their cytoplasmic domains would be
separated by over 100 Å. This interaction could inhibit signaling
in the absence of TNF. Parallel dimers are also observed in which the
dimer interface is well separated from the TNF binding site.
Associations among TNF-bound parallel dimers could cause receptor
clustering. Both dimers bury substantial areas of protein surface and
are formed by polar and non-polar interactions.
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