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interleukin-1 receptor antagonist protein (IRAP) 399 interleukin-1 receptor deficiency
Human IL1β-converting enzyme (x-ray diffraction; resolution = 2.6 Å).
NH 2
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COOH
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COOH
Type I Type II
NH 2
Interleukin-1 receptors, types I and II.
an extracellular portion that binds ligand and contains all
N-linked glycosylation sites. A 217-amino-acid segment,
apparently confined to the cytoplasm, may be involved in
signal transduction. Further studies of ligand binding have
been facilitated through the development of a soluble form
of the cloned IL1R molecule that contains the extracellular
part but not the transmembrane cytoplasmic region of the
molecule. IL1α and IL1β molecules bind with equivalent
affinities. It has been claimed that the IL1R has more than
one subunit based on the demonstration of bands, such as
Backbone structure of human interleukin-1β revealed by NMR.
Interleukin-1 receptor antagonist protein (resolution = 3.2 Å).
a 100-kDa band, in addition to that characteristic of the
receptor which is 80 kDa. Recombinant IL1R functions in
signal transduction. When the cytoplasmic part of the IL1R
is depleted, the molecule does not function. The human
T cell IL1R has been cloned and found to be similar to its
murine counterpart. Two affinity classes of binding sites for
IL1 have been described.
interleukin-1 receptor antagonist protein (IRAP)
A substance on T lymphocytes and endothelial cells that
inhibits IL1 activity.
interleukin-1 receptor deficiency
CD4 + T cells deficient in IL1 receptors in affected individuals
fail to undergo mitosis when stimulated and fail to generate
IL2. This leads to a lack of immune responsiveness and constitutes
a type of combined immunodeficiency. Opportunistic
I