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Updated: Jan 31, 2026
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Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
Published on: June 15, 2019
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Solution structure of TT30, a novel complement therapeutic agent, provides insight into its joint binding to
Keying Li1, Jayesh Gor, V Michael Holers
1Department of Structural and Molecular Biology, Darwin Building, University College London, Gower Street, London WC1E 6BT, UK.
Journal of Molecular Biology
|March 6, 2012
Summary
A novel therapeutic reagent, TT30, shows an elongated structure and limited flexibility, enabling effective binding to complement C3b and C3d for treating complement-mediated diseases.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- The alternative complement pathway is implicated in various diseases.
- Novel therapeutic reagents targeting complement are needed.
Purpose of the Study:
- To determine the solution structure of the novel therapeutic reagent TT30.
- To understand how TT30 binds to complement C3b and C3d.
Main Methods:
- Analytical ultracentrifugation
- X-ray scattering
- Constrained molecular modeling
- Structural analysis of CR2-C3d complex
Main Results:
- TT30 exhibits an elongated monomeric structure with limited inter-SCR flexibility.
- TT30's structure allows its complement factor H domains to bind C3b while CR2 domains extend freely.
- TT30 readily interacts with C3d ligands in multiple orientations when bound to C3b.
Conclusions:
- The determined solution structure of TT30 provides insights into its binding mechanism.
- TT30's structural characteristics support its potential as a therapeutic agent for complement-related disorders.
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