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Related Experiment Video

Updated: Nov 20, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Properdin oligomers adopt rigid extended conformations supporting function.

Dennis V Pedersen¹, Martin Nors Pedersen², Sofia Mm Mazarakis¹

¹Department of Molecular Biology and Genetics, Center for Structural Biology, Aarhus University, Aarhus, Denmark.

|January 22, 2021

Summary

This summary is machine-generated.

Properdin oligomers are rigid and extended, influencing immune system complement cascade function. Their specific structure, not just multivalency, is crucial for biological activity.

Keywords:

MD simulation SAXS complement electron microscopy human immunology inflammation molecular biophysics protease structural biology

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Last Updated: Nov 20, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Published on: May 13, 2020

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

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Published on: February 6, 2020

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

Immunology
Structural Biology
Biophysics

Background:

Properdin stabilizes complement cascade convertases, crucial for immune responses.
Properdin's biological activity is linked to its oligomerization state.
The structural properties and rigidity of properdin oligomers remain poorly understood.

Purpose of the Study:

To investigate the structural conformations of properdin oligomers.
To determine the relationship between properdin oligomer structure and its function in complement activation.

Main Methods:

Electron microscopy
Solution scattering techniques
Cell lysis assays

Main Results:

Properdin oligomers adopt extended, rigid conformations (230-360 Å).
Monomers are pretzel-shaped; dimers are curved; trimers/tetramers are planar.
Multivalency alone does not guarantee full properdin activity.

Conclusions:

Properdin oligomers possess well-defined, rigid structures.
The extended oligomer conformation is integral to properdin's function in the complement cascade.
Simultaneous binding via all sites is unlikely for trimers and tetramers.