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La isomerización rápida peptídica cis-trans dentro de las colgajas flexibles ricas en Gly de la proteasa VIH-1
Donald Hamelberg1, J Andrew McCammon
1Howard Hughes Medical Institute, Center for Theoretical Biological Physics, Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093, USA. dhamelbe@mccammon.ucsd.edu
Journal of the American Chemical Society
|October 6, 2005
Resumen
La proteasa del VIH-1 es el VIH-1.
Área de la Ciencia:
- Biología molecular La biología molecular.
- La biofísica es la biofísica.
- Biología estructural Biología estructural.
Sus antecedentes:
- La proteasa del virus de la inmunodeficiencia humana tipo 1 (VIH-1) es esencial para la replicación viral.
- Su sitio activo está regulado por solapas flexibles, pero el mecanismo atomístico de esta flexibilidad sigue sin estar claro.
- Comprender la dinámica del colgajo es crucial para desarrollar terapias antivirales efectivas.
Objetivo del estudio:
- Para dilucidar el mecanismo atomistic detrás de la flexibilidad de los colgajos de proteasa del VIH-1.
- Investigar el papel de las regiones ricas en glicina y los enlaces peptídicos específicos en la dinámica de las aletas.
- Explorar el impacto de las estructuras secundarias en la cinética de los procesos moleculares.
Principales métodos:
- Simulaciones computacionales para analizar la dinámica molecular.
- Investigando la isomerización cis-trans de los enlaces Gly-Gly omega.
- Estudiar la formación del bucle peptídico y su efecto en las tasas de isomerización.
Principales resultados:
- El enlace omega Gly-Gly en las puntas de los colgajos ricos en glicina de la proteasa VIH-1 exhibe una isomerización cis-trans inusualmente rápida.
- Esta rápida isomerización ocurre en la escala de tiempo de microsegundos a milisegundos, significativamente más rápido que las tasas típicas.
- La estructura de bucle beta-hairpin de las puntas de las aletas se identifica como la causa de esta isomerización acelerada.
Conclusiones:
- La flexibilidad de los colgajos de la proteasa del VIH-1 es impulsada por la rápida isomerización del enlace Gly-Gly.
- La formación de un bucle de beta-hairpin en las puntas de las aletas acelera inesperadamente este proceso de isomerización.
- Estos hallazgos proporcionan nuevos conocimientos sobre los mecanismos dinámicos de las proteasas virales y los posibles objetivos farmacológicos.
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