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Related Concept Videos

Antibody Structure01:10

Antibody Structure

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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...
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Antibody Structure and Classes01:25

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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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Immunoglobulin-like Cell Adhesion Molecules01:31

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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.
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Structure of Cadherins01:25

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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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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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Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization
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Immunoglobulin Structure Exhibits Control over CDR Motion.

Michael T Zimmermann1, Aris Skliros2, Andrzej Kloczkowski3

  • 1L. H. Baker Center for Bioinformatics and Biological Statistics, Iowa State University, Ames, IA 50011, USA ; Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA ; Bioinformatics and Computational Biology, Iowa State University, Ames, IA 50011, USA.

Immunome Research
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Summary
This summary is machine-generated.

Immunoglobulin G (IgG) hinge motions are crucial for antigen binding, with its structure facilitating large movements of antigen-binding domains. This design enables efficient information transfer for effective antibody function.

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Area of Science:

  • Structural biology
  • Immunology
  • Computational biophysics

Background:

  • The immunoglobulin G (IgG) structure's flexibility is critical for its function in antigen binding.
  • Understanding internal motions and hinge dynamics is key to elucidating IgG's mechanism of action.

Purpose of the Study:

  • To investigate how IgG hinge motions facilitate antigen binding.
  • To analyze the influence of protein environment on experimental temperature factors.
  • To evaluate the spatial sampling and internal motions of IgG domains.

Main Methods:

  • Normal mode analysis (NMA) of an elastic network model (ENM) was employed.
  • Analysis focused on identifying hinges, low-frequency modes, and dominant internal motions.
  • Protein crystal and packing effects on temperature factors were assessed.

Main Results:

  • IgG hinge motions and antigen-binding domains exhibit large spatial sampling, crucial for function.
  • Crystallographic temperature factors can be misleading regarding specific functional motions.
  • The full IgG structure demonstrates more efficient information transfer than individual Fab domains.

Conclusions:

  • The IgG structure is specifically designed to facilitate antigen binding through large domain excursions.
  • Normal mode analysis effectively predicts hinge motions and spatial sampling.
  • Coupling of antigen-binding loops with large-scale hinge motions enhances antibody efficacy.