Video Experimental Relacionado

Updated: Jul 8, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

Published on: August 15, 2014

La estructura cristalina del receptor humano de IgE de alta afinidad

S C Garman¹, J P Kinet, T S Jardetzky

¹Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.

|January 6, 1999

Resumen

Los investigadores han determinado la estructura 3D del receptor humano de alta afinidad IgE, revelando su interacción con IgE. Esta visión estructural es clave para desarrollar nuevos tratamientos para la alergia.

Área de la Ciencia:

Inmunología Inmunología.
Biología Estructural Biología estructural.
La bioquímica es la bioquímica.

Sus antecedentes:

Las respuestas alérgicas son desencadenadas por la activación de los mastocitos a través del receptor humano de alta afinidad IgE.
Las reacciones mediadas por IgE requieren la unión de IgE a su receptor de alta afinidad para su iniciación.

Objetivo del estudio:

Determinar la estructura cristalina de rayos X de los dominios de unión de anticuerpos del receptor IgE humano.
Proporcionar una base estructural para el desarrollo de nuevas terapias para la alergia.

Principales métodos:

Se empleó cristalografía de rayos X para resolver la estructura.
La estructura se determinó con una resolución de 2,4 Å.

Principales resultados:

La estructura reveló una disposición muy doblada de los dominios de inmunoglobulina.
Se identificó una superficie convexa extendida para la interacción de IgE.
Se observó un bucle específico que confiere la especificidad de IgE y una disposición inusual de triptófano.

Conclusiones:

La estructura cristalina determinada ofrece una base molecular para comprender la función del receptor de IgE.
Esta información estructural puede guiar el diseño de nuevas terapias antialérgicas dirigidas al receptor IgE.

Más Videos Relacionados

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Published on: February 6, 2017

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Videos de Conceptos Relacionados

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

Gene Families

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

Transcytosis of IgG

Transcytosis of IgG

Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

Antibody Structure and Classes

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.