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Related Concept Videos

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...
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Cytoskeletal Accessory Proteins01:13

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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
Protein Complexes with Interchangeable Parts01:57

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Structure of Cadherins01:25

Structure of Cadherins

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 diversity of cadherins...
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...

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Related Experiment Video

Updated: Jun 18, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

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Published on: November 28, 2017

Structure of complement receptor 2 in complex with its C3d ligand.

G Szakonyi1, J M Guthridge, D Li

  • 1Department of Biochemistry and Molecular Genetics, University of Colorado Health Science Center, School of Medicine, Denver, CO 80262, USA.

Science (New York, N.Y.)
|June 2, 2001
PubMed
Summary

Researchers detailed the X-ray structure of Complement Receptor 2 (CR2) bound to C3d. This reveals key interactions, offering insights for designing new drugs targeting immune responses.

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09:39

Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)

Published on: September 17, 2019

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Complement receptor 2 (CR2/CD21) is crucial for B lymphocyte activation.
  • CR2 bridges innate and adaptive immunity, interacting with ligands like C3d and EBV glycoprotein.
  • Understanding CR2-ligand interactions is vital for immune system modulation.

Purpose of the Study:

  • To elucidate the structural basis of the interaction between CR2 and its ligand C3d.
  • To provide atomic-level detail of the CR2-C3d complex.
  • To identify potential targets for molecular drug design.

Main Methods:

  • X-ray crystallography was employed to determine the structure.
  • The structure of the CR2 domain in complex with C3d was resolved at 2.0 angstrom resolution.

Main Results:

  • The X-ray structure reveals extensive main chain interactions between C3d and a single short consensus repeat (SCR) of CR2.
  • Substantial side-side packing was observed within the SCRs of CR2.
  • Detailed molecular interactions at the interface were characterized.

Conclusions:

  • The study provides a detailed understanding of CR2-ligand interactions.
  • The findings highlight potential molecular targets for therapeutic intervention.
  • This structural insight can guide the development of novel drugs modulating immune responses.