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La estructura de una interacción adhesiva de la tirosina fosfatasa revela un mecanismo de abrazadera espaciadora
A Radu Aricescu1, Christian Siebold, Kaushik Choudhuri
1Cancer Research UK Receptor Structure Research Group, University of Oxford, Henry Wellcome Building of Genomic Medicine, Division of Structural Biology, Roosevelt Drive, Oxford OX3 7BN, UK.
Science (New York, N.Y.)
|September 1, 2007
Resumen
El RPTPmu humano, una proteína tirosina fosfatasa, forma un dímero rígido que actúa como una regla molecular. Esta estructura ayuda a regular la adhesión célula-célula mediante el control de la distancia entre las células en las uniones de adherencias.
Área de la Ciencia:
- Biología celular Biología celular.
- Biología estructural Biología estructural.
- La bioquímica es la bioquímica.
Sus antecedentes:
- Los contactos célula-célula son cruciales para los organismos multicelulares.
- RPTPmu humano es una proteína receptor tirosina fosfatasa involucrada en la regulación de la adhesión celular.
- Se desfosforila los complejos de cadherina-catenina.
Objetivo del estudio:
- Para determinar la estructura cristalina del ectodominio RPTPmu.
- Comprender las bases estructurales del papel de RPTPmu en la adhesión celular.
- Para investigar cómo RPTPmu regula el espaciamiento intercelular.
Principales métodos:
- Cristalografía de rayos X (resolución de 3.1 angstroms).
- Análisis de la estructura y la dimerización del ectodominio RPTPmu.
- La expresión de la superficie celular de construcciones de deleción para medir el espaciamiento intercelular.
Principales resultados:
- El ectodominio RPTPmu forma un dimero homófilo trans (antiparalelo) homófilo.
- El dímero exhibe una arquitectura extendida y rígida, que coincide con las dimensiones de unión de las adherencias.
- Los espacios intercelulares inducidos por construcciones de deleción se correlacionan con la longitud del ectodominio.
Conclusiones:
- El ectodominio RPTPmu funciona como un medidor de distancia.
- Desempeña un papel regulador clave en el posicionamiento de la fosfatasa en las uniones de adherencia.
- Esta visión estructural aclara el mecanismo de RPTPmu en el control de la adhesión celular.
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