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Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer
Sirik R Leliveld1, Mathieu H M Noteborn, Jan Pieter Abrahams
1Department of Chemistry, Leiden University, The Netherlands.
European Journal of Biochemistry
|August 16, 2003
Summary
Recombinant apoptin protein, a tumor-killing agent, forms stable multimers. These complexes have a stable core structure essential for their tumor-selective apoptosis-inducing activity.
Area of Science:
- Molecular Biology
- Biochemistry
- Cancer Research
Background:
- Recombinant apoptin protein exhibits selective apoptosis induction in human tumor cells.
- Apoptin is isolated as a stable multimeric complex.
- The protein complex displays biological activity despite apparent structural disorder.
Purpose of the Study:
- To investigate the structural properties of recombinant apoptin multimers.
- To elucidate the relationship between apoptin structure and its biological activity.
- To propose a model for the apoptin multimer structure.
Main Methods:
- Characterization of recombinant apoptin protein complex.
- Analysis of subunit conformation and exchange dynamics.
- Hydrophobic interaction studies.
Main Results:
- Apoptin exists as a stable multimer of 30-40 monomers.
- The multimer exhibits uniform hydrophobic patches and stable domains.
- A small fraction of subunits are exchangeable, suggesting a stable core structure.
Conclusions:
- Apoptin multimers possess a stable core of nonexchangeable subunits.
- Exchangeable subunits are attached via hydrophobic interactions.
- The stable core structure is proposed as the biologically active form of apoptin.