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3D domain swapping: a mechanism for oligomer assembly
M J Bennett1, M P Schlunegger, D Eisenberg
1Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059, USA.
Protein Science : a Publication of the Protein Society
|December 1, 1995
Summary
3D domain swapping allows proteins to form complex structures by exchanging parts between identical chains. This process can alter protein function and potentially drive the evolution of new protein assemblies.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- 3D domain swapping is a process where proteins exchange domains to form oligomers.
- This swapping can involve large globular domains or smaller structural elements like helices or strands.
Purpose of the Study:
- To review examples of 3D domain swapping.
- To explore its role in functional interconversion between monomeric and oligomeric states.
- To investigate its potential role in the evolution of oligomeric proteins.
Main Methods:
- Review of existing literature and protein structural data.
- Analysis of protein structures exhibiting domain swapping.
- Comparative analysis of monomeric and oligomeric forms.
Main Results:
- 3D domain swapping results in intertwined dimers or higher-order oligomers.
- The swapped domains can vary significantly in size.
- Domain swapping can lead to proteins adopting multiple distinct structures from a single chain.
Conclusions:
- 3D domain swapping is a versatile mechanism for protein oligomerization.
- It provides a pathway for functional plasticity and evolutionary innovation in proteins.
- Domain-swapped proteins exemplify structural adaptability.