Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Complement System

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...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Cryo-electron Microscopy

Cryo-electron Microscopy

Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...

You might also read

Related Articles

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

Sort by

Same author

A potential mechanism for tetraspanin CD82-mediated regulation of EGFR.

Life science alliance·2026

Same author

Exome sequencing enables molecular diagnosis in 10% of early-onset or familial systemic lupus erythematosus cases.

EBioMedicine·2026

Same author

Molecular driving force of a small molecule-induced protein disorder-order transition.

Communications chemistry·2026

Same author

Structural insights into C3 convertase activity of the classical pathway of complement.

Nature communications·2025

Same author

The fc fragment of IgMs binds C1q to activate the first step of the classical complement pathway, while inhibiting complement-dependent cytotoxicity.

The FEBS journal·2025

Same author

CD70 recruitment to the immunological synapse is dependent on CD20 in B cells.

Proceedings of the National Academy of Sciences of the United States of America·2025

Search research articles

Related Experiment Video

Updated: Jul 12, 2026

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Deciphering complement mechanisms: the contributions of structural biology.

Gérard J Arlaud¹, Paul N Barlow, Christine Gaboriaud

¹Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France. arlaud@ibs.fr

Molecular Immunology

|September 5, 2007

Summary

Structural biology techniques like X-ray crystallography and NMR have revealed the atomic-level mechanisms of the complement system. This understanding aids in designing targeted inhibitors for complement functions.

More Related Videos

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

Related Experiment Videos

Last Updated: Jul 12, 2026

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

Area of Science:

Immunology
Structural Biology
Biochemistry

Background:

The complement system, a crucial part of innate immunity, plays a vital role in host defense and inflammation.
Structural biology has been instrumental in elucidating the molecular intricacies of complement components since 1980.
Approximately a hundred complement structures were available in the Protein Data Bank by early 2007.

Purpose of the Study:

To review the significant contributions of structural biology to understanding the complement system.
To illustrate how X-ray crystallography and NMR techniques reveal complement mechanisms at the atomic level.
To highlight the implications of structural insights for the rational design of complement inhibitors.

Main Methods:

X-ray crystallography
Nuclear Magnetic Resonance (NMR) spectroscopy
Analysis of Protein Data Bank (PDB) entries

Main Results:

Detailed atomic-level understanding of complement component structures and functions.
Elucidation of sophisticated molecular mechanisms underlying complement activation and regulation.
Identification of potential targets for therapeutic intervention through structure-based drug design.

Conclusions:

Structural biology approaches have profoundly advanced the comprehension of the complement system.
Atomic-level structural data provides a foundation for developing specific complement inhibitors.
Continued structural studies are essential for further deciphering complement functions and therapeutic applications.