Title: Implications of 3D domain swapping for protein folding, misfolding and function
Authors: Rousseau, Frederic ×
Schymkowitz, Joost
Itzhaki, Laura S #
Issue Date: Sep-2012
Publisher: Plenum Press
Series Title: Advances in Experimental Medicine and Biology vol:747 issue:1 pages:137-52
Abstract: 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-swapping 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.
ISSN: 0065-2598
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Switch Laboratory
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science