Structure and mechanism of interleukin-lβ converting enzyme
KP Wilson, JAF Black, JA Thomson, EE Kim, JP Griffith… - Nature, 1994 - nature.com
Interleukin-lβ converting enzyme (ICE) processes an inactive precursor to the
proinflammatory cytokine, interleukin-lβ, and may regulate programmed cell death in
neuronal cells. The high-resolution structure of human ICE in complex with an inhibitor has
been determined by X-ray diffraction. The structure confirms the relationship between
human ICE and cell-death proteins in other organisms. The active site spans both the 10
and 20K subunits, which associate to form a tetramer, suggesting a mechanism for ICE …
proinflammatory cytokine, interleukin-lβ, and may regulate programmed cell death in
neuronal cells. The high-resolution structure of human ICE in complex with an inhibitor has
been determined by X-ray diffraction. The structure confirms the relationship between
human ICE and cell-death proteins in other organisms. The active site spans both the 10
and 20K subunits, which associate to form a tetramer, suggesting a mechanism for ICE …
Abstract
Interleukin-lβ converting enzyme (ICE) processes an inactive precursor to the proinflammatory cytokine, interleukin-lβ, and may regulate programmed cell death in neuronal cells. The high-resolution structure of human ICE in complex with an inhibitor has been determined by X-ray diffraction. The structure confirms the relationship between human ICE and cell-death proteins in other organisms. The active site spans both the 10 and 20K subunits, which associate to form a tetramer, suggesting a mechanism for ICE autoactivation.
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