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Bases estructurales para la unión de nucleótidos de DNP y purina a la UCP1
Yunlu Kang1, Lei Chen2,3,4,5
1State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing, China.
Nature
|June 19, 2023
Resumen
La proteína de desacoplamiento 1 (UCP1) facilita la producción de calor al conducir protones a través de la membrana mitocondrial interna. Los estudios estructurales revelan cómo los ácidos grasos y los nucleótidos como el ATP se unen a UCP1, explicando sus mecanismos de activación e inhibición.
Área de la Ciencia:
- Biología mitocondrial
- Biología estructural
- La bioquímica
Sus antecedentes:
- La proteína de desacoplamiento 1 (UCP1) es crucial para la termogénesis, separando la respiración de la síntesis de ATP.
- La actividad de UCP1 está modulada por ácidos grasos y nucleótidos de purina, pero los mecanismos de unión no están claros.
Objetivo del estudio:
- Para aclarar los mecanismos moleculares de unión del ligando a la UCP1 humana.
- Determinar la base estructural para la activación de la UCP1 por los ácidos grasos y la inhibición por el ATP.
Principales métodos:
- Se utilizó la cristalografía de rayos X para determinar las estructuras de la UCP1 humana.
- Se obtuvieron estructuras para estados libres de nucleótidos, ligados a DNP y ligados a ATP de UCP1.
Principales resultados:
- El UCP1 humano posee una cavidad central abierta accesible desde el citosol.
- El 2,4-dinitrofenol (DNP) se une a las hélices transmembrana TM2 y TM6.
- El ATP se une al mismo sitio que el DNP, induciendo cambios conformacionales e inhibiendo el transporte de protones.
Conclusiones:
- El ATP inhibe competitivamente la unión de DNP al ocupar el sitio activo de UCP1.
- Las ideas estructurales explican la regulación de UCP1 por los ácidos grasos y los nucleótidos.
- Esto proporciona una base para comprender la función de UCP1 en la regulación metabólica.
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