How do proteins build bonds? This review delves into the intriguing world of three-dimensional (3D) domain swapping, a process where proteins exchange identical domains to form a bond between two or more molecules. The study of domain-swapped proteins has expanded since it was first identified in diphtheria toxin. This research explores the diversity of swapped domains, focusing on primary and secondary structures found at the N or C terminus. Several case studies provide a detailed look at 3D domain swapping, including proteins that swap more than one domain, evidence in amyloid proteins, and the flexibility of hinge loops. Furthermore, the paper discusses the physiological relevance and a potential mechanism for this process. Ultimately, the authors suggest that 3D domain swapping can occur in any protein with an unconstrained terminus under the right conditions, setting a framework for future findings and highlighting the potential for manipulation to influence protein function. This review provides a comprehensive overview of current knowledge and offers a framework for understanding future discoveries.
Published in Protein Science, this paper on 3D domain swapping aligns with the journal's focus on protein structure, function, and folding. By exploring the mechanisms and implications of domain swapping, the research contributes to a deeper understanding of protein interactions and their roles in biological processes. The extensive list of references indicates a strong connection to other studies in protein science.
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