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Bases estructurales para la unión de péptidos ricos en prolina a los dominios SH3

H Yu¹, J K Chen, S Feng

¹Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138.

|March 11, 1994

Resumen

Los dominios SH3 se unen a motivos ricos en prolina mediante el reconocimiento de una conformación específica de hélice de poliprolina zurda. Los principales residuos de prolina forman la hélice, mientras que otros y los residuos no prolinos confieren especificidad.

Área de la Ciencia:

Biología Molecular Biología Molecular
Biología Estructural Biología estructural.
La bioquímica es la bioquímica.

Sus antecedentes:

Los dominios SH3 son módulos cruciales de interacción de las proteínas.
Se sabe que los motivos ricos en prolina interactúan con los dominios SH3.
Comprender estas interacciones es clave para la función de las proteínas.

Objetivo del estudio:

Para identificar motivos comunes en los ligandos que se unen a los dominios SH3.
Para determinar la base estructural de las interacciones dominio-ligando SH3.
Para aclarar el papel de los residuos específicos en la afinidad de unión y la especificidad.

Principales métodos:

Selección de la biblioteca de péptidos combinatorios sesgados. selección de la biblioteca de péptidos combinatorios.
Determinación de la estructura de la solución de un complejo de ligandos SH3.
Mutagénesis dirigida al sitio del dominio y el ligando SH3.
Pruebas de afinidad de unión. ensayos de afinidad de unión.

Principales resultados:

Se identificó un motivo RXL común en los ligandos ricos en prolina.
La estructura de la solución reveló una conformación de hélice de poliprolina (PPII) tipo II de izquierda.
Las mutaciones afectaron la unión, destacando la importancia de los residuos de prolina y los residuos específicos de no prolina (arginina, leucina).

Conclusiones:

Los dominios SH3 reconocen motivos ricos en prolina que adoptan una hélice PPII.
Los residuos de prolina son esenciales para la formación de hélices y el contacto con los receptores.
Los residuos de no prolina contribuyen a la especificidad del ligando.

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