Chapter Category: Protein

From the book Protein Dimerization (and Oligomerization) in Biology

Implications of 3D Domain Swapping for Protein Folding, Misfolding and Function

Frederic Rousseau, Joost Schymkowitz and Laura Itzhaki

Three‑dimensional domain swapping is the process by which two identical protein chains exchange a part of their structure to form an intertwined dimer or higher‑order oligomer. The phenomenon has been observed in the crystal structures of a range of different proteins. In this chapter we review the experiments that have been performed in order to understand the sequence and structural determinants of domain‑ wapping and these show how the general principles obtained can be used to engineer proteins to domain swap. We discuss the role of domain swapping in regulating protein function and as one possible mechanism of protein misfolding that can lead to aggregation and disease. We also review a number of interesting pathways of macromolecular assembly involving β‑strand insertion or complementation that are related to the domain swapping phenomenon.

Taken from the book

Protein Dimerization (and Oligomerization) in Biology

Edited by: Jacqui Matthews

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