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La estructura cristalina del dominio de reconocimiento de la fosfotirosina SH2 de v-src complejo con péptidos
G Waksman1, D Kominos, S C Robertson
1Rockefeller University, New York.
Nature
|August 20, 1992
Resumen
El oncogén de la v-src.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Estructural Biología estructural.
- Oncología Oncología.
Sus antecedentes:
- El producto del oncogén v-src es una tirosina quinasa implicada en el cáncer.
- Los dominios SH2 son críticos para mediar las interacciones proteína-proteína que involucran la fosforilación de tirosina.
- Comprender estas interacciones es clave para desarrollar terapias dirigidas.
Objetivo del estudio:
- Para dilucidar la estructura tridimensional del dominio SH2 del producto oncogénico v-src.
- Caracterizar las interacciones de unión entre el dominio SH2 y los péptidos fosfotirosil.
Principales métodos:
- Se empleó cristalografía de rayos X para determinar las estructuras.
- Se recopilaron datos de alta resolución (1.5 y 2.0 A) para dos complejos.
Principales resultados:
- La estructura del dominio SH2 presenta una hoja beta antiparalela central flanqueada por hélices alfa.
- La unión al péptido ocurre en la hoja beta, los bucles y una hélice alfa.
- El reconocimiento específico de la fosfotirosina implica enlaces de hidrógeno e interacciones amino-aromáticas (lisina, arginina).
Conclusiones:
- Las estructuras determinadas proporcionan información detallada sobre el reconocimiento del péptido SH2 dominio-fosfotirosilo.
- Esta información estructural puede informar el diseño de inhibidores dirigidos a las vías de señalización v-src.
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