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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...
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.
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Antibody Structure01:10

Antibody Structure

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...
Antibody Structure01:10

Antibody Structure

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...
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...
Antibody Structure and Classes01:25

Antibody Structure and Classes

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.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

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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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Functional anatomy of complement factor H.

Elisavet Makou1, Andrew P Herbert, Paul N Barlow

  • 1School of Chemistry, University of Edinburgh, Edinburgh EH9 3JJ, U.K.

Biochemistry
|May 25, 2013
PubMed
Summary
This summary is machine-generated.

Factor H (FH) protects the body from complement-mediated injury by regulating inflammatory pathways. Understanding FH

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Last Updated: May 11, 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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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
  • Complement System Biology
  • Molecular Medicine

Background:

  • Factor H (FH) is a key regulator of the vertebrate complement system, preventing host tissue damage.
  • Dysregulation of FH is linked to diseases like age-related macular degeneration and atypical hemolytic uremic syndrome.
  • Pathogens can exploit FH for their own defense mechanisms.

Purpose of the Study:

  • To review the emerging molecular understanding of Factor H function.
  • To explore the structural and functional characteristics of FH.
  • To discuss proposed models of FH activation and regulation.

Main Methods:

  • Literature review and synthesis of existing data on Factor H.
  • Analysis of structural and functional studies.
  • Reconciliation of historical data with recent findings.

Main Results:

  • Progress in characterizing FH's three-dimensional architecture and intermodular flexibility.
  • Models proposed for FH activation by C3b on self-surfaces.
  • Identification of FH's role in modulating complement amplification.

Conclusions:

  • A deeper molecular understanding of FH is developing.
  • Proposed models link FH sequence variations to disease pathophysiology.
  • Further quantitative assays and data analysis are needed to validate FH function models.