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Related Concept Videos

Complement System01:27

Complement System

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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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.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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Antimicrobial Proteins01:23

Antimicrobial Proteins

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Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
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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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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Antibody Actions01:26

Antibody Actions

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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
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Updated: Mar 6, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

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Structural Implications for the Formation and Function of the Complement Effector Protein iC3b.

Malvina Papanastasiou1, Sophia Koutsogiannaki1, Yiannis Sarigiannis1

  • 1Department of Pathology and Laboratory Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104; and.

Journal of Immunology (Baltimore, Md. : 1950)
|March 5, 2017
PubMed
Summary
This summary is machine-generated.

The complement system

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • The complement system is crucial for host defense and homeostasis.
  • The complement activation fragment iC3b is a key effector molecule.
  • High-resolution structural data for iC3b and its dynamics are lacking.

Purpose of the Study:

  • To determine the high-resolution structure and dynamics of iC3b.
  • To compare the structure and dynamics of iC3b with its parent protein C3b.
  • To elucidate the structural basis for iC3b's effector functions and recognition patterns.

Main Methods:

  • Hydrogen-deuterium exchange mass spectrometry (HDX-MS) was employed.
  • HDX-MS provided peptide-level resolution of protein structure and dynamics.
  • Structural findings were validated using a specific anti-iC3b monoclonal antibody (mAb).

Main Results:

  • HDX-MS analysis covered almost the entire 173-kDa iC3b protein.
  • iC3b exhibits increased deuterium uptake in several regions compared to C3b, indicating higher flexibility and solvent exposure.
  • The CUB domain of iC3b is highly disordered, resembling intrinsically disordered proteins, leading to significant structural flexibility.

Conclusions:

  • iC3b possesses a highly flexible structure, particularly in its CUB domain.
  • This structural flexibility likely underlies iC3b's effector functions and interactions with complement regulators and receptors.
  • The study provides crucial structural insights into the complement system's activation fragment iC3b.