Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Antibody Structure01:10

Antibody Structure

67.1K
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...
67.1K
Antibody Structure01:10

Antibody Structure

15.1K
15.1K
Gene Families01:57

Gene Families

10.2K
Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
10.2K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

48.2K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
48.2K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.9K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.9K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
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...
3.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Studies on Pathological Changes in the Gastrointestinal Tract Due to Helminth Infection in Backyard Chickens.

Journal of parasitology research·2026
Same author

The fT3/fT4 ratio as a candidate marker of motor progression in SCA3.

Neurobiology of disease·2026
Same author

One-step synthesis of Zolpidem and its analogues <i>via</i> visible light induced coupling of imidazo[1,2-α]pyridines with 2-bromoacetamides.

Organic & biomolecular chemistry·2026
Same author

Nongenetic Factors Associated with Age at Onset and Disease Severity in Spinocerebellar Ataxia Type 3: A Cross-Sectional Cohort Study.

Movement disorders : official journal of the Movement Disorder Society·2026
Same author

The ERβ Agonist, OSU-ERβ-012, Mitigates Inflammation in a Chimeric Model of Systemic Lupus Erythematosus.

ACR open rheumatology·2026
Same author

Aspirin-induced mesenchymal stem cell-derived extracellular vesicles promote osteochondral regeneration by reprogramming macrophages.

Biomaterials·2026

Related Experiment Video

Updated: Mar 18, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

12.0K

Crystal structure of zebrafish complement 1qA globular domain.

Hongyu Yuan1, Rong Chen1, Mansoor Tariq1

  • 1Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, People's Republic of China.

Protein Science : a Publication of the Protein Society
|July 9, 2016
PubMed
Summary

The first non-mammalian structure of zebrafish C1qA globular domain reveals differences in immune molecule binding compared to humans. This finding offers insights into the evolutionary path of C1qA proteins from ancient ancestors.

Keywords:
C1q globular domainevolutionstructurezebrafish

More Related Videos

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

12.3K
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

13.3K

Related Experiment Videos

Last Updated: Mar 18, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

12.0K
High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

12.3K
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

13.3K

Area of Science:

  • Immunology
  • Structural Biology
  • Evolutionary Biology

Background:

  • C1q, a key component of the classical complement system, features globular domains (C1qgD) essential for immune function.
  • C1qgD facilitates interactions with immune molecules like immunoglobulin G (IgG) and C-reactive protein (CRP), crucial for host defense.

Purpose of the Study:

  • To determine the structure of the zebrafish C1qA globular domain (Dare-C1qAgD).
  • To compare the structural features and potential binding sites of zebrafish C1qA with its human counterpart.
  • To elucidate the evolutionary relationship between fish and human C1qA proteins.

Main Methods:

  • X-ray crystallography was employed to solve the three-dimensional structure of Dare-C1qAgD.
  • Comparative structural analysis was performed between Dare-C1qAgD and human C1qA structures.

Main Results:

  • The overall architecture of Dare-C1qAgD is conserved compared to human C1qA.
  • Specific residues involved in binding C1qB, C1qC, and CRP show variations between zebrafish and human C1qA.
  • Key residues for IgG binding present in human C1qA are absent in zebrafish C1qA.

Conclusions:

  • The structural differences highlight potential variations in immune molecule interactions between fish and mammals.
  • The study provides valuable insights into the molecular evolution of C1qA from a common ancestral protein.
  • Dare-C1qAgD structure serves as a crucial reference for understanding complement system evolution in vertebrates.