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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...
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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
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...
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...

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Related Experiment Video

Updated: Jun 26, 2026

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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The structural basis of the multiple forms of human complement component C4.

K T Belt, M C Carroll, R R Porter

    Cell
    |April 1, 1984
    PubMed
    Summary

    Researchers sequenced human complement components C4A and C4B alleles, revealing the complete amino acid sequence for C4 precursor and secreted forms. This study identified nucleotide differences between C4A and C4B, and within C4A alleles.

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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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    Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry
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    Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry

    Published on: May 19, 2020

    Area of Science:

    • Immunology
    • Molecular Biology
    • Genetics

    Background:

    • Human complement components C4A and C4B are crucial for immune response.
    • These components are highly polymorphic, with significant implications for immune function and disease susceptibility.
    • Understanding their genetic variations is essential for immunological research.

    Purpose of the Study:

    • To determine the complete amino acid sequence of human complement C4 precursor and secreted forms.
    • To identify nucleotide sequence differences between C4A and C4B alleles.
    • To investigate allelic variations within the C4A gene.

    Main Methods:

    • Preparation of cDNA clones from human liver mRNA of a heterozygous donor.
    • Sequencing of C4A allele cDNA to derive amino acid sequences.
    • Comparative analysis of C4A and C4B allele sequences.

    Main Results:

    • The complete amino acid sequence of the 1722-residue C4 single chain precursor was determined.
    • Estimated amino acid sequences for the three peptide chains of secreted C4 were obtained.
    • Tentative identification of nucleotide sequence differences between C4A and C4B, and allelic differences within C4A.

    Conclusions:

    • The study provides a comprehensive amino acid sequence for human complement C4.
    • Identified sequence variations contribute to the understanding of C4A/C4B and C4A allelic polymorphism.
    • These findings advance the molecular understanding of the human complement system.