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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.
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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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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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Antigen Processing Pathways01:31

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MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Updated: Feb 21, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

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A peptide extension dictates IgM assembly.

Dzana Pasalic1, Benedikt Weber1, Chiara Giannone2

  • 1Center for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, 85748 Garching, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|October 5, 2017
PubMed
Summary
This summary is machine-generated.

The tailpiece peptide extension on IgM heavy chains is essential for correct antibody assembly. A disulfide bond in the tailpiece triggers conformational changes, driving the formation of complex IgM polymers for immune defense.

Keywords:
IgM structureantibodydisulfide bond linkageimmunoglobulin foldprotein complex assembly

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Area of Science:

  • Immunology
  • Molecular Biology
  • Structural Biology

Background:

  • Secretory cells produce complex molecules like IgM antibodies, crucial for the immune system's first line of defense.
  • Polymeric IgM antibodies are highly effective due to their multivalency in combating pathogens.

Purpose of the Study:

  • To elucidate the molecular mechanisms governing the biosynthesis and assembly of polymeric IgM antibodies.
  • To identify the specific structural elements and processes responsible for correct IgM complex formation.

Main Methods:

  • Investigated IgM biosynthesis in living cells.
  • Reconstituted IgM assembly processes in vitro.
  • Utilized alanine scanning mutagenesis to analyze the function of the IgM heavy chain tailpiece.

Main Results:

  • A conserved C-terminal peptide extension, the tailpiece, is necessary and sufficient for correct IgM geometry.
  • Hydrophobic amino acids in the tailpiece's first half are critical for establishing proper topology.
  • Disulfide bond formation between tailpieces initiates assembly, inducing conformational changes that drive polymerization.

Conclusions:

  • IgM polymerization is dictated by a local conformational switch within the tailpiece peptide extension.
  • This mechanism enables the biogenesis of large and structurally complex IgM antibody assemblies.