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Domain swapping and amyloid fibril conformation

Van Der Wel, PCA (2012) Domain swapping and amyloid fibril conformation. Prion, 6 (3). 211 - 216. ISSN 1933-6896

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For several different proteins an apparent correlation has been observed between the propensity for dimerization by domain-swapping and the ability to aggregate into amyloid-like fibrils. Examples include the disease-related proteins beta2-microglobulin and transthyretin. This has led to proposals that the amyloid-formation pathway may feature extensive domain swapping. One possible consequence of such an aggregation pathway is that the resulting fibrils would incorporate structural elements that resemble the domain-swapped forms of the protein and, thus, reflect certain native-like structures or domain-interactions. In magic angle spinning solid-state NMR-based and other structural studies of such amyloid fibrils, it appears that many of these proteins form fibrils that are not native-like. Several fibrils instead have an in-register, parallel conformation, which is a common amyloid structural motif and is seen, for instance, in various prion fibrils. Such a lack of native structure in the fibrils suggests that the apparent connection between domain-swapping ability and amyloid-formation may be more subtle or complex than may be presumed at first glance. © 2012 Landes Bioscience.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Van Der Wel, PCApvdwel@pitt.eduPVDWEL0000-0002-5390-3321
Date: 1 July 2012
Date Type: Publication
Journal or Publication Title: Prion
Volume: 6
Number: 3
Page Range: 211 - 216
DOI or Unique Handle: 10.4161/pri.18987
Schools and Programs: School of Medicine > Structural Biology
Refereed: Yes
ISSN: 1933-6896
Article Type: Review
Date Deposited: 28 Sep 2017 14:00
Last Modified: 14 Oct 2017 09:55


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