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Estructura cristalina de la proteasa cisteína de la enzima de conversión beta de la interleucina-1: a (p20/p10) 2
N P Walker1, R V Talanian, K D Brady
1BASF Aktiengesellschaft, Main Laboratory, Ludwigshafen, Federal Republic of Germany.
Cell
|July 29, 1994
Resumen
La enzima de conversión beta de la interleucina-1 (ICE) es una proteasa crucial para la apoptosis. Su estructura cristalina revela un homodímero de dominios catalíticos, lo que sugiere nuevos conocimientos sobre las vías programadas de muerte celular.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Molecular Biología Molecular
- Biología Estructural Biología estructural.
Sus antecedentes:
- La enzima de conversión beta de la interleucina-1 (ICE, por sus siglas en inglés) divide proteolíticamente la pro-IL-1 beta en su forma activa.
- ICE es homólogo al producto genético de la muerte celular de C. elegans, CED-3.
- Los miembros de la familia ICE/CED-3 están implicados en la muerte celular programada (apoptosis).
Objetivo del estudio:
- Para determinar la estructura cristalina de un complejo de clorometilcetonas humanas ICE-tetrapeptido recombinante.
- Para aclarar la base estructural del ensamblaje y la activación de la holoenzima ICE.
- Investigar las similitudes funcionales dentro de la familia de proteasas ICE/CED-3.
Principales métodos:
- Cristalografía de rayos X con una resolución de 2.5 A.
- Análisis de un complejo de clorometilcetonas de tetrapeptido ICE recombinante humano.
Principales resultados:
- La holoenzima es un homodímero de dominios catalíticos, cada uno compuesto de subunidades p20 y p10.
- La separación espacial del extremo C de p20 y el extremo N de p10 sugiere vías alternativas de ensamblaje y activación in vivo.
- La conservación de los residuos del sitio activo entre los miembros de la familia ICE/CED-3 indica mecanismos funcionales compartidos.
Conclusiones:
- La estructura cristalina proporciona información sobre la organización homodímera del ICE.
- Los hallazgos sugieren nuevas vías para el ensamblaje y la activación de ICE in vivo.
- ICE y CED-3 representan una nueva clase de proteasas cisteína citoplasmáticas cruciales para la apoptosis.
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