Crystal structure and mutants of interleukin-1.beta. converting

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase

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435 24, 435212, 435219, 435226, C12Q 137

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060571195

ABSTRACT:
Interleukin-1.beta. converting enzyme ("ICE") processes an inactive precursor to the pro-inflammatory cytokine, interleukin-1.beta.. The high-resolution structure of human ICE crystallized in complex with an inhibitor is determined by X-ray diffraction. The active site spans both the 10 and 20 kilodalton subunits. The accessory binding site is composed of residues from the p10 and p20 subunits that are adjacent to the two-fold axis of the crystal. The structure coordinates of the enzyme may be used to design novel classes of ICE inhibitors.

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