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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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Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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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.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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Selectins01:25

Selectins

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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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...
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Updated: Jul 15, 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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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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Structural biology of complement receptors.

Jorge Santos-López1, Karla de la Paz1,2, Francisco J Fernández2

  • 1Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain.

Frontiers in Immunology
|September 27, 2023
PubMed
Summary

The complement system, vital for immunity and inflammation, involves receptors crucial in various diseases. This review details the structural biology of complement receptors and their complexes, guiding future research.

Keywords:
C5aR1/C5L2/C3aRCR1/CR2CR3/CR4CRIgcomplementcomplement receptorshost-pathogen interactionsstructural biology

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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Medicine

Background:

  • The complement system is integral to immune responses and implicated in numerous diseases.
  • Complement receptors (CRs) are key mediators of complement-driven immunity and cross-talk between innate and adaptive immunity.
  • Understanding CR structure is crucial for deciphering their function and therapeutic potential.

Purpose of the Study:

  • To review the current knowledge on the structural biology of complement receptors and their complexes.
  • To highlight fundamental concepts, research gaps, and challenges in the field.
  • To provide guidance for future research in complement structural biology.

Main Methods:

  • Literature review focusing on structural biology studies of complement receptors.
  • Analysis of structural data for complement receptors, their natural ligands, and pharmacological modulators.
  • Synthesis of information on structural features, functional implications, and therapeutic relevance.

Main Results:

  • Detailed description of the structural classes and features of eight major complement receptors.
  • Elucidation of structural complexes formed by CRs with agonists and antagonists.
  • Identification of current research gaps and areas requiring further investigation.

Conclusions:

  • Structural insights into complement receptors are fundamental for understanding immune processes and developing therapeutics.
  • Further structural studies are needed to address existing knowledge gaps and unlock therapeutic potential.
  • The field is poised for advancements with potential future developments in complement system research.