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Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

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Definición de las interacciones interfaciales del homodímero de ubiquitina no covalente a través de comparaciones con

Nicole D Wagner¹, David H Russell¹

¹Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.

Journal of the American Chemical Society

|December 16, 2016

Resumen

Los dímeros de ubiquitina no covalentes muestran similitudes estructurales con la diubiquitina ligada a K48. Estos hallazgos sugieren interacciones hidrofóbicas similares tanto en los dímeros de ubiquitina vinculados a K48 como en los no covalentes.

Área de la Ciencia:

La bioquímica
Biología estructural
Espectrometría de masas

Sus antecedentes:

La diubiquitina (diUbq) vinculada covalentemente exhibe distintas interacciones interfaciales basadas en el tipo de enlace (K48 frente a K63).
El obstáculo estérico del cable covalente influye en estas interacciones.

Objetivo del estudio:

Investigar las preferencias estructurales y las interacciones interfaciales de los dímeros de ubiquitina no covalentes.
Para comparar estas propiedades con la diubiquitina conocida vinculada a K48 y K63.

Principales métodos:

Espectrometría de masas de movilidad de iones desplegables inducida por colisión (CIU-IM-MS).

Principales resultados:

Los dímeros de ubiquitina no covalentes muestran preferencias estructurales.
Las interacciones interfaciales de los dímeros no covalentes se parecen mucho a las de la diubiquitina ligada a K48.
Las interacciones hidrofóbicas son predominantes en los dímeros no covalentes, similares al K48-diUbq.

Conclusiones:

Los dímeros de ubiquitina no covalentes comparten similitudes estructurales e interaccionales con la diubiquitina ligada a K48.
Esto sugiere una posible convergencia en la base estructural de ciertas vías de señalización de la ubiquitina.

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