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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 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.
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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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An adult in good health typically has between 4,500 and 11,000 leukocytes, or white blood cells, per microliter of blood, which constitutes about 1% of the total blood volume. Unlike red blood cells, white blood cells contain a nucleus and other cellular organelles but do not have hemoglobin. Most white blood cells reside in connective tissues, particularly in lymphatic organs such as the lymph nodes, with only a small fraction present in circulating blood.
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Related Experiment Video

Updated: Dec 21, 2025

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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Emerging Insights into the Structure and Function of Complement C5a Receptors.

Shubhi Pandey1, Jagannath Maharana1, Xaria X Li2

  • 1Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur 208016, India.

Trends in Biochemical Sciences
|May 14, 2020
PubMed
Summary

Complement factor C5a binds two receptors, C5aR1 and C5aR2, initiating immune responses. Recent studies reveal structural differences and functional bias, explaining how C5aR2 mimics atypical chemokine receptors.

Keywords:
G protein-coupled receptorsbiased agonismcomplement C5afunctional biasligand–receptor interactionsβ-arrestins

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • The complement cascade, particularly C5a, is crucial for innate immunity.
  • C5a exerts functions through C5aR1 and C5aR2, which exhibit distinct signaling properties.
  • C5aR1 is a typical GPCR, while C5aR2 lacks G protein coupling but recruits β-arrestins.

Purpose of the Study:

  • To review recent structural and functional studies of C5a-receptor interactions.
  • To explore the concept of functional bias in the C5aR system.
  • To discuss the analogy between C5aR2 and atypical chemokine receptors (ACKRs).

Main Methods:

  • Analysis of recent structural biology data on ligand-receptor interactions.
  • Review of functional assays investigating transducer coupling (G proteins, β-arrestins).
  • Comparative analysis of C5aR2 with ACKRs.

Main Results:

  • Direct structural insights into C5a-C5aR1 and C5a-C5aR2 binding.
  • Evidence for functional bias, with differing signaling outcomes despite a common agonist.
  • Identification of structural motifs correlating with distinct transducer recruitment.

Conclusions:

  • The functional divergence of C5aR1 and C5aR2 is underpinned by structural differences and biased signaling.
  • C5aR2 shares functional similarities with ACKRs, suggesting a broader role beyond classical complement signaling.
  • Further research is needed to fully elucidate the mechanistic basis of C5aR functional divergence.