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Related Concept Videos

Complement System01:27

Complement System

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 membrane...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Complex Assembly02:41

Protein Complex Assembly

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: May 13, 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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Dimerization of complement factor H-related proteins modulates complement activation in vivo.

Elena Goicoechea de Jorge1, Joseph J E Caesar, Talat H Malik

  • 1Centre for Complement and Inflammation Research, Department of Medicine, Imperial College, London W12 0NN, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|March 15, 2013
PubMed
Summary

The complement system

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Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

Area of Science:

  • Immunology and Molecular Biology
  • Structural Biology

Background:

  • The complement system is crucial for immune responses but its dysregulation is linked to diseases like age-related macular degeneration.
  • Genomic variations in the complement factor H-related (CFHR) locus are associated with complement-mediated diseases.
  • The precise biological functions of CFHR proteins remain poorly understood, hindering mechanistic insights into these diseases.

Purpose of the Study:

  • To investigate the structural properties and biological role of complement factor H-related (CFHR) proteins.
  • To elucidate the mechanism by which CFHR proteins modulate complement system activity.
  • To explain the link between CFHR variation and susceptibility to specific diseases.

Main Methods:

  • Unique structural data analysis of three CFHR proteins.
  • Investigation of protein dimerization capabilities (homodimers and heterodimers).
  • Assessment of ligand binding avidity and competition with complement factor H (CFH).

Main Results:

  • Three CFHR proteins possess a shared dimerization motif, enabling homodimer and heterodimer formation.
  • Dimerization enhances avidity for complement fragments, allowing CFHR proteins to compete with CFH.
  • CFHR proteins act as competitive antagonists of CFH, modulating complement activation in vivo.

Conclusions:

  • CFHR proteins function as competitive antagonists of complement factor H.
  • Protein dimerization is a key structural property enabling CFHRs to regulate complement activation.
  • Understanding CFHR dimerization explains their role in diseases associated with complement dysregulation.