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Structure and mechanism of interleukin-lβ converting enzyme

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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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Authors and Affiliations

  1. Vertex Pharmaceuticals Incorporated, 40 Allston Street, Cambridge, Massachusetts, 02139, USA

    Keith P. Wilson, Jo-Anne F. Black, John A. Thomson, Eunice E. Kim, James P. Griffith, Manuel A. Navia, Mark A. Murcko, Stephen P. Chambers, Robert A. Aldape, Scott A. Raybuck & David J. Livingston

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  1. Keith P. Wilson
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  2. Jo-Anne F. Black
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  3. John A. Thomson
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  4. Eunice E. Kim
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  6. Manuel A. Navia
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  7. Mark A. Murcko
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Wilson, K., Black, JA., Thomson, J. et al. Structure and mechanism of interleukin-lβ converting enzyme. Nature 370, 270–275 (1994). https://doi.org/10.1038/370270a0

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  • DOI: https://doi.org/10.1038/370270a0

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