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Related Experiment Video

Updated: May 22, 2026

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

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Published on: March 5, 2018

The modular serine proteases of the complement cascade.

Federico Forneris¹, Jin Wu, Piet Gros

¹Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.

Current Opinion in Structural Biology

|May 8, 2012

Summary

This summary is machine-generated.

Modular serine proteases in the mammalian immune system activate through complex protein interactions. Understanding these structural changes is key to how the complement cascade recognizes and clears pathogens.

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Area of Science:

Immunology
Structural Biology
Biochemistry

Background:

Modular serine proteases are crucial components of the mammalian humoral immune system.
These proteases function within large protein complexes, relying on multi-domain interactions for proteolytic activity.

Purpose of the Study:

To review structural insights into the complement cascade.
To elucidate the mechanisms of complement initiation, amplification, and regulation.

Main Methods:

Review of structural data on complement proteases.
Analysis of protein complex formation and domain rearrangements.

Main Results:

Complement initiation involves auto-activation of hetero-tetrameric proteases within danger-recognition complexes.
Amplification occurs via C3 convertase formation, labeling particles for clearance.
Regulation involves convertase dissociation and degradation to prevent host tissue damage.

Conclusions:

Complex formation and large domain rearrangements are fundamental to complement cascade proteolysis.
These processes enable the host to identify and eliminate microbes and cellular debris.