Video Experimental Relacionado

Updated: Jan 25, 2026

Determination of Molecular Structures of HIV Envelope Glycoproteins using Cryo-Electron Tomography and Automated Sub-tomogram Averaging

Determination of Molecular Structures of HIV Envelope Glycoproteins using Cryo-Electron Tomography and Automated Sub-tomogram Averaging

Published on: December 1, 2011

Base molecular del receptor de alfavirus artrogénico MXRA8 que se une a la proteína de la envoltura del virus del

Hao Song¹, Zhennan Zhao², Yan Chai³

¹Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China.

|May 14, 2019

Resumen

El virus del chikungunya (CHIKV) utiliza el receptor MXRA8 para entrar en las células. Los estudios estructurales revelan que MXRA8 se une al CHIKV

Área de la Ciencia:

Virología y Biología Estructural
Mecanismos moleculares de la entrada del virus

Sus antecedentes:

Los alfavirus artrogénicos, incluido el virus de Chikungunya (CHIKV), causan una morbilidad global significativa y una carga económica debido a las enfermedades reumáticas.
MXRA8 ha sido identificado recientemente como un receptor de entrada celular crítico para CHIKV.
Comprender las interacciones moleculares entre CHIKV y MXRA8 es crucial para el desarrollo de terapias antivirales.

Objetivo del estudio:

Para aclarar la base estructural de la unión de CHIKV a su receptor, MXRA8.
Proporcionar información a nivel atómico sobre la interfaz de interacción para la identificación de objetivos terapéuticos.

Principales métodos:

Se empleó la cristalografía de rayos X para determinar las estructuras del MXRA8 de ratón, el MXRA8 humano complejo con la proteína CHIKV E y las partículas similares al virus CHIKV unidas al MXRA8 humano.
La criomicroscopia electrónica proporcionó datos estructurales de alta resolución del complejo MXRA8-CHIKV.

Principales resultados:

MXRA8 posee dos dominios Ig-como con topologías estructurales distintas.
El receptor se une dentro de un " cañón " formado por protómeros de proteína CHIKV E en la superficie del virión.
Las interacciones atómicas involucran tanto los dominios MXRA8 como la región de bisagra con residuos CHIKV E1-E2, y la región del tallo es vital para la entrada del virus.

Conclusiones:

La comprensión estructural detallada de la interacción MXRA8-CHIKV proporciona una base para el diseño de estrategias antivirales dirigidas.
La identificación del papel crítico de la región del tallo MXRA8 ofrece una nueva vía para la intervención terapéutica contra el CHIKV y los alfavirus relacionados.

Palabras clave:

MXRA8 (en inglés)molécula de adhesión el virus alfa artrogénico El virus del chikungunya Enlace de recepción Entrada del virus

Más Videos Relacionados

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

Videos de Conceptos Relacionados

G-protein Coupled Receptors

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

What are Viruses?

What are Viruses?

Internal Receptors

Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.

G Protein-coupled Receptors

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...