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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
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Glycosylation Modulates Human CD2-CD58 Adhesion via Conformational Adjustment
Xingyu Wang1, Chang G Ji2,3,1, John Z H Zhang2,3,1,4
1§NYU-ECNU Center for Computational Chemistry at NYU Shanghai, Shanghai 200062, China.
The Journal of Physical Chemistry. B
|May 19, 2015
Summary
Glycosylation of human CD2 (a cell surface protein) stabilizes its binding with CD58 by altering the protein's conformation. This molecular mechanism is crucial for immune cell adhesion and recognition.
Area of Science:
- Immunology
- Molecular Biology
- Biophysics
Background:
- Human CD2 is a cell surface glycoprotein on T lymphocytes and NK cells, vital for immune recognition.
- CD2 interacts with CD58, mediating adhesion between immune cells like T lymphocytes and antigen-presenting cells.
Purpose of the Study:
- To investigate the molecular impact of glycosylation on the CD2-CD58 adhesion complex structure and dynamics.
- To elucidate the mechanism by which glycosylation regulates CD2-CD58 binding.
Main Methods:
- Molecular dynamics (MD) simulations were employed to analyze the CD2-CD58 complex.
- Detailed analysis focused on the structural and dynamic effects of glycosylation on CD2.
Main Results:
- The CD2-CD58 interaction is stabilized by three key 'hot spots' forming a critical binding triangle.
- Glycosylation significantly influences the conformation of human CD2, optimizing the binding triangle topology.
- This conformational steering by glycosylation energetically stabilizes the CD2-CD58 complex.
Conclusions:
- Glycosylation of human CD2 promotes CD2-CD58 binding through conformational adjustments.
- The findings elucidate the dynamic mechanism of glycosylation in controlling cell adhesion.
- Results align with experimental data, enhancing understanding of immune recognition processes.
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