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Updated: Jun 16, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

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Structure of human desArg-C5a.

William J Cook¹, Nicholas Galakatos, William C Boyar

¹University of Alabama at Birmingham, Birmingham, AL 35294, USA. wjcook@uab.edu

Acta Crystallographica. Section D, Biological Crystallography

|February 4, 2010

Summary

This summary is machine-generated.

The complement C5a protein, crucial in inflammation, shows a different structure in crystal form compared to NMR studies. This desArg-C5a dimer reveals a three-helix core, differing from the previously known four-helix bundle.

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Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Published on: August 16, 2017

Area of Science:

Biochemistry
Structural Biology
Immunology

Background:

Anaphylatoxin C5a, derived from complement component C5, plays a key role in inflammatory disease pathogenesis.
Previous Nuclear Magnetic Resonance (NMR) structures of human and porcine C5a revealed a four-helix bundle stabilized by disulfide bonds.

Purpose of the Study:

To determine the crystal structure of human desArg-C5a.
To compare the crystal structure with existing NMR structures and identify structural differences.

Main Methods:

X-ray crystallography was used to determine the structure of human desArg-C5a in two crystal forms.
Structural analysis and comparison with NMR-derived structures.

Main Results:

Human desArg-C5a crystallizes as a dimer.
Each monomer exhibits a three-helix core, distinct from the four-helix bundle observed in NMR structures.
The N-terminal helices of the monomers are positioned differently compared to NMR structures, and differ from each other.

Conclusions:

The crystal structure of human desArg-C5a reveals a novel dimeric form with a three-helix core.
Significant structural discrepancies exist between the crystal and NMR structures, particularly concerning the helical bundle and N-terminal helix positioning.
The physiological relevance of these observed structural differences requires further investigation.