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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...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Mechanism of Ciliary Motion01:05

Mechanism of Ciliary Motion

The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
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...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

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Related Experiment Video

Updated: Jul 11, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

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

Published on: June 15, 2019

Complement C1q-target proteins recognition is inhibited by electric moment effectors.

Lubka Roumenina1, Svetlana Bureeva, Alexander Kantardjiev

  • 1Department of Biochemistry, Sofia University, St. Kliment Ohridski, 8 Dragan Tsankov St., Sofia 1164, Bulgaria.

Journal of Molecular Recognition : JMR
|October 12, 2007
PubMed
Summary

New disulphate compounds inhibit the classical complement pathway by targeting the C1q globular domain. These compounds disrupt C1q

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Last Updated: Jul 11, 2026

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Published on: August 21, 2017

Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • The classical complement pathway is vital for innate immunity but can cause tissue damage if overactivated.
  • Understanding complement activation and inhibition is crucial for biomedical applications.
  • C1q binding to targets initiates the classical pathway, a process influenced by calcium and electric moments.

Purpose of the Study:

  • To elucidate the mechanism by which low molecular weight disulphate compounds inhibit C1q.
  • To investigate how these inhibitors interact with the globular (gC1q) domain of C1q.

Main Methods:

  • Experimental assays to test inhibitor efficacy.
  • Computational docking to model C1q-inhibitor interactions.
  • Theoretical modeling to understand the biophysical mechanisms involved.

Main Results:

  • Betulin disulphate (B2S) and F2S inhibit C1q interaction with IgG1, CRP, and PTX3.
  • Inhibitors alter electric/dipole moment vectors, reducing electrostatic steering and target recognition.
  • Inhibitors likely block the conformational change of C1q required for complement activation.

Conclusions:

  • Disulphate compounds effectively inhibit classical complement pathway initiation by targeting C1q.
  • Inhibition occurs by disrupting C1q's electric moment, impairing target binding and conformational changes.
  • These findings suggest a novel class of 'electric moment inhibitors' for therapeutic development.