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Proteins ; 83(7): 1297-306, 2015 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-25921217

RESUMEN

Salpichrolides are natural plant steroids that contain an unusual six-membered aromatic ring D. We recently reported that some of these compounds, and certain analogs with a simplified side chain, exhibited antagonist effects toward the human estrogen receptor (ER), a nuclear receptor whose endogenous ligand has an aromatic A ring (estradiol). Drugs acting through the inhibition or modulation of ERs are frequently used as a hormonal therapy for ER(+) breast cancer. Previous results suggested that the aromatic D ring was a key structural motif for the observed activity; thus, this modified steroid nucleus may provide a new scaffold for the design of novel antiestrogens. Using molecular dynamics (MD) simulation we have modeled the binding mode of the natural salpichrolide A and a synthetic analog with an aromatic D ring within the ERα. These results taken together with the calculated energetic contributions associated to the different ligand-binding modes are consistent with a preferred inverted orientation of the steroids in the ligand-binding pocket with the aromatic ring D occupying a position similar to that observed for the A ring of estradiol. Major changes in both dynamical behavior and global positioning of H11 caused by the loss of the ligand-His524 interaction might explain, at least in part, the molecular basis of the antagonism exhibited by these compounds. Using steered MD we also found a putative unbinding pathway for the steroidal ligands through a cavity formed by residues in H3, H7, and H11, which requires only minor changes in the overall receptor conformation.


Asunto(s)
Ergosterol/análogos & derivados , Estradiol/química , Moduladores de los Receptores de Estrógeno/química , Receptor alfa de Estrógeno/antagonistas & inhibidores , Simulación del Acoplamiento Molecular , Relación Estructura-Actividad , Secuencias de Aminoácidos , Sitios de Unión , Ergosterol/síntesis química , Ergosterol/química , Moduladores de los Receptores de Estrógeno/síntesis química , Receptor alfa de Estrógeno/química , Humanos , Ligandos , Simulación de Dinámica Molecular , Datos de Secuencia Molecular , Unión Proteica , Estructura Secundaria de Proteína , Estructura Terciaria de Proteína , Termodinámica , Interfaz Usuario-Computador
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