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Related Concept Videos

Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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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.
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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.
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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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.
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Related Experiment Video

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Structures of human γδ T cell receptor-CD3 complex.

Weizhi Xin1,2,3, Bangdong Huang1,2,3, Ximin Chi1,2,3,4

  • 1Research Center for Industries of the Future, Center for Infectious Disease Research, Zhejiang Key Laboratory of Structural Biology, School of Life Sciences, Westlake University, Hangzhou, China.

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Gamma delta T cell receptors (TCRs) associate with CD3 subunits to activate immune responses. This study reveals distinct Vγ usage dictates TCR-CD3 complex assembly, influencing T cell activation and immunotherapy potential.

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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Biology

Background:

  • Gamma delta (γδ) T cells are a unique T cell subgroup critical for immune responses and immunopathology.
  • The γδ T cell receptor (TCR) recognizes antigens independently of the major histocompatibility complex and associates with CD3 subunits for T cell activation.
  • γδ TCR-CD3 complexes hold significant potential for immunotherapy.

Purpose of the Study:

  • To elucidate the distinct structural mechanisms of human Vγ9Vδ2 and Vγ5Vδ1 TCR-CD3 complexes.
  • To understand how Vγ usage influences TCR-CD3 assembly and T cell activation.
  • To provide insights into γδ TCR properties for advancing immunotherapeutic strategies.

Main Methods:

  • X-ray crystallography to determine the structures of Vγ9Vδ2 and Vγ5Vδ1 TCR-CD3 complexes.
  • Biochemical and biophysical assays to validate structural findings and assess functional implications.
  • Analysis of conformational flexibility, transmembrane interactions, and oligomeric states.

Main Results:

  • The Vγ9Vδ2 TCR-CD3 complex is monomeric with flexible extracellular domains and connecting peptides, regulated by a cholesterol-like molecule in the transmembrane region.
  • The Vγ5Vδ1 TCR-CD3 complex exhibits a dimeric architecture stabilized by Vγ5 domain interactions, which is crucial for T cell activation.
  • Two distinct assembly mechanisms for γδ TCR-CD3 complexes are revealed, dependent on Vγ usage.

Conclusions:

  • The study reveals fundamental organizing principles of γδ TCR-CD3 complex assembly.
  • Distinct structural conformations of γδ TCR-CD3 complexes dictate their function and T cell activation.
  • These findings offer valuable insights for developing targeted immunotherapies.