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Engineering an intertwined form of CD2 for stability and assembly
A J Murray1, J G Head, J J Barker
1Department of Biochemistry and Centre for Molecular Recognition, University of Bristol, University Walk, UK.
Nature Structural Biology
|September 10, 1998
Summary
The CD2 protein
Area of Science:
- Protein structure and folding
- Molecular evolution
- Biochemistry
Background:
- The amino-terminal domain of CD2 can fold as a monomer or a metastable dimer.
- Understanding protein folding flexibility is crucial for protein design.
Purpose of the Study:
- To investigate the differential stabilization of CD2 protein folds.
- To explore protein assembly capabilities through sequence engineering.
Main Methods:
- Engineering the CD2 sequence to mimic mutagenesis.
- Determining crystal structures of a hinge-deletion mutant.
Main Results:
- Engineered CD2 variants exhibit stabilized monomeric or dimeric folds.
- Crystal structures reveal domain rotations enabling tetramer formation.
- A single polypeptide sequence can adopt diverse folds.
Conclusions:
- Protein sequence engineering can control CD2 folding pathways.
- The study provides insights into designing proteins for self-assembly.