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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Immunoglobulin-like Cell Adhesion Molecules01:31

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...
Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
T Cell Activation and Clonal Selection01:22

T Cell Activation and Clonal Selection

T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
Naive T cells that have not yet encountered an antigen express two primary CD...
Cytotoxic T Cells-mediated Immune Response01:27

Cytotoxic T Cells-mediated Immune Response

Cytotoxic T cells are a vital component of the immune system. They have the remarkable ability to identify and target antigens on infected or abnormal cells. These antigens often originate from intracellular pathogens such as viruses or abnormal proteins cancer cells produce.
Immunological surveillance is the ability of immune cells to monitor and eliminate infected cells with intracellular pathogens, neoplastically transformed cells, and cells with non-self antigens. Cytotoxic T cells and NK...
B Cell Activation and Differentiation01:24

B Cell Activation and Differentiation

The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...

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Related Experiment Video

Updated: May 11, 2026

Real-time Live Imaging of T-cell Signaling Complex Formation
10:31

Real-time Live Imaging of T-cell Signaling Complex Formation

Published on: June 23, 2013

Structural basis for co-stimulation by the human CTLA-4/B7-2 complex.

J C Schwartz1, X Zhang, A A Fedorov

  • 1[1] Department of Microbiology and Immunology, [2] These authors contributed equally to this work.

Nature
|March 30, 2001
PubMed
Summary
This summary is machine-generated.

The structure of CTLA-4 (cytotoxic T-lymphocyte-associated protein 4) and B7-2 interaction reveals how T-cell responses are regulated. This finding provides insights into immune modulation and potential therapeutic targets.

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Visualizing the Actin and Microtubule Cytoskeletons at the B-cell Immune Synapse Using Stimulated Emission Depletion (STED) Microscopy

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Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
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Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation

Published on: February 28, 2019

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Last Updated: May 11, 2026

Real-time Live Imaging of T-cell Signaling Complex Formation
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Visualizing the Actin and Microtubule Cytoskeletons at the B-cell Immune Synapse Using Stimulated Emission Depletion (STED) Microscopy
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Visualizing the Actin and Microtubule Cytoskeletons at the B-cell Immune Synapse Using Stimulated Emission Depletion (STED) Microscopy

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Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
12:09

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation

Published on: February 28, 2019

Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Medicine

Background:

  • T-cell activity relies on co-stimulatory signals from CD28 and CTLA-4 receptors.
  • CD28 engagement stimulates T-cells, while CTLA-4 engagement attenuates the response.
  • CTLA-4 and CD28 pathways are key targets for autoimmune diseases, graft rejection, and cancer immunotherapy.

Purpose of the Study:

  • To elucidate the structural basis of CTLA-4 and B7-2 interaction.
  • To understand the cell-surface organization of these receptor/ligand complexes.
  • To provide a molecular model for T-cell signaling regulation.

Main Methods:

  • Determined the 3.2-Å resolution crystal structure of the human CTLA-4 dimer complexed with the human B7-2 receptor-binding domain.

Main Results:

  • The structure revealed unusual dimerization of CTLA-4 and B7-2, with ligand-binding sites distal to the dimer interface.
  • Observed an alternating arrangement of bivalent CTLA-4 and B7-2 dimers, forming an extended network.
  • This network suggests a model for molecular organization within the immunological synapse.

Conclusions:

  • The CTLA-4/B7-2 network structure provides a model for periodic organization in the immunological synapse.
  • This structure suggests a unique signaling mechanism for dimeric cell-surface receptors.
  • Understanding this interaction is crucial for developing targeted immunotherapies.