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Related Concept Videos

Complementation Tests00:49

Complementation Tests

A complementation test is a simple cross to identify whether the two mutations are located on the same gene or different genes. It was first performed by Edward Lewis in the 1940s while working on fruit flies. He developed the test to identify the location and arrangement of different mutations on chromosomes.
Organisms heterozygous for different mutations are crossed pairwise in all combinations. If present on different genes, the mutations can complement each other by providing the missing...
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...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles, paraspeckles, etc. These nuclear...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
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The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

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Updated: May 18, 2026

Functional Complementation Analysis (FCA): A Laboratory Exercise Designed and Implemented to Supplement the Teaching of Biochemical Pathways
09:27

Functional Complementation Analysis (FCA): A Laboratory Exercise Designed and Implemented to Supplement the Teaching of Biochemical Pathways

Published on: June 24, 2016

Putting the structure into complement.

Susan M Lea1, Steven Johnson

  • 1Sir William Dunn School of Pathology, South Parks Road, Oxford OX1 3RE, UK. susan.lea@path.ox.ac.uk

Immunobiology
|September 12, 2012
PubMed
Summary
This summary is machine-generated.

New structural insights into the complement system reveal critical regulatory events. Understanding these molecular frameworks, especially transient cell surface assemblies, is key to advancing complement biology.

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Last Updated: May 18, 2026

Functional Complementation Analysis (FCA): A Laboratory Exercise Designed and Implemented to Supplement the Teaching of Biochemical Pathways
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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Biology

Background:

  • The complement system is crucial for innate immunity and inflammation.
  • Understanding complement regulation is vital for treating immune-related diseases.
  • Recent advances in structural biology have begun to elucidate complement pathways.

Purpose of the Study:

  • To review key protein structures of the complement system determined recently.
  • To highlight insights gained into complement regulatory mechanisms.
  • To identify outstanding questions requiring structural data for resolution.

Main Methods:

  • Review of recently published structural data (X-ray crystallography, cryo-EM).
  • Analysis of protein-protein interactions within complement assemblies.
  • Integration of structural findings with functional data.

Main Results:

  • New structures illuminate critical regulatory events in complement activation.
  • Insights into transient assemblies at the cell surface provide a dynamic view.
  • Structural data reveals mechanisms of complement evasion by pathogens.

Conclusions:

  • Recent structural studies have significantly advanced our understanding of complement regulation.
  • Further structural work is needed to address remaining questions in complement biology.
  • Molecular frameworks are essential for future therapeutic strategies targeting the complement system.