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La base estructural para el secuestro de los motivos celulares LxxLL por el papilomavirus E6 en las oncoproteínas
Katia Zanier1, Sebastian Charbonnier, Abdellahi Ould M'hamed Ould Sidi
1Biotechnologie et Signalisation Cellulaire UMR 7242, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, BP 10413, F-67412 Illkirch, France.
Science (New York, N.Y.)
|February 9, 2013
Resumen
Las oncoproteínas del virus del papiloma E6 impulsan los tumores epiteliales al unirse a las proteínas del huésped a través de motivos LxxLL. El análisis estructural revela un bolsillo conservado crucial para la actividad oncogénica y la multifuncionalidad de E6.
Área de la Ciencia:
- Biología estructural Biología estructural.
- Virología Virología.
- Investigación de la investigación del cáncer.
Sus antecedentes:
- Las oncoproteínas virales E6 son críticas en los tumores epiteliales inducidos por el papilomavirus, como el cáncer cervical humano.
- Las proteínas E6 interactúan con las proteínas del huésped a través de motivos ácidos específicos LxxLL.
Objetivo del estudio:
- Para aclarar la base estructural de las interacciones de la proteína E6 con motivos LxxLL.
- Comprender el papel de la bolsa de unión LxxLL en la actividad oncogénica y multifuncionalidad de E6.
Principales métodos:
- Se utilizó cristalografía de rayos X para determinar las estructuras del virus del papiloma bovino E6 (BPV1) y del virus del papiloma humano E6 (HPV16) unidos a los péptidos LxxLL.
- El análisis estructural se centró en la interacción entre los dominios de zinc E6, la hélice de enlace y los motivos helicoidales LxxLL.
Principales resultados:
- Las estructuras cristalinas revelaron que las proteínas BPV1 y HPV16 E6 poseen un bolsillo básico-hidrofóbico formado por dominios de zinc y una hélice de enlace.
- Este bolsillo tiene motivos helicoidales LxxLL, lo que sugiere un mecanismo de unión conservado.
- La inactivación mutacional de esta bolsa abolió las actividades oncogénicas de ambas proteínas E6.
Conclusiones:
- El estudio revela la base estructural para la multifuncionalidad y la oncogenia de las proteínas del papilomavirus E6.
- El identificado bolsillo de unión LxxLL es esencial para el papel de E6 en el desarrollo de tumores.
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