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La estructura de la proteasa 3C del rinovirus humano revela un pliegue de polipéptido parecido a la tripsina, un

D A Matthews¹, W W Smith, R A Ferre

¹Agouron Pharmaceuticals, San Diego, California 92121.

|June 3, 1994

Resumen

Se determinó la estructura de la proteasa 3C del rinovirus humano-14, revelando similitudes y diferencias con las proteasas serinas. Esto proporciona información sobre la replicación viral y los posibles objetivos terapéuticos.

Área de la Ciencia:

Biología estructural Biología estructural.
Virología Virología.
La bioquímica es la bioquímica.

Sus antecedentes:

La proteasa 3C (3Cpro) del rinovirus humano-14 es esencial para la replicación viral.
Comprender su estructura es clave para desarrollar estrategias antivirales.

Objetivo del estudio:

Para determinar la estructura de alta resolución del rinovirus humano-14 3C proteasa.
Para comparar sus características estructurales con otras proteasas, particularmente las proteasas serinas.
Investigar posibles mecanismos para el procesamiento de poliproteínas y la unión al ARN.

Principales métodos:

Se utilizó la cristalografía de rayos X para determinar la estructura 3D.
La estructura fue refinada a una resolución de 2.3 Å con un factor R de 0.22.

Principales resultados:

La estructura 3Cpro consiste en dos barriles beta de seis hebras topológicamente equivalentes.
Los residuos catalíticos (Cys-146, His-40, Glu-71) se conservan, pero el agujero de oxyanión se reposiciona.
Los residuos de unión al ARN se encuentran alejados del sitio activo.
Las interacciones de la red cristalina sugieren un modelo para la escisión intermolecular de la poliproteína 3CD.

Conclusiones:

La proteasa 3C del rinovirus humano-14 comparte similitudes estructurales con las proteasas serinas similares a la tripsina, pero tiene características distintas.
El agujero de oxyanión reposicionado y los sitios de unión de ARN distantes pueden influir en la especificidad del sustrato y la interacción del ARN viral.
Los hallazgos ofrecen una base estructural para comprender la función de 3Cpro en el procesamiento de poliproteínas virales y sugieren posibles vías para el diseño de fármacos antivirales.

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