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Complete structure of an epithelial keratin dimer: implications for intermediate filament assembly

Bray, David J., Walsh, Tiffany R., Noro, Massimo G. and Notman, Rebecca 2015, Complete structure of an epithelial keratin dimer: implications for intermediate filament assembly, PLoS one, vol. 10, no. 7, Article Number : e0132706, pp. 1-22, doi: 10.1371/journal.pone.0132706.

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Title Complete structure of an epithelial keratin dimer: implications for intermediate filament assembly
Author(s) Bray, David J.
Walsh, Tiffany R.ORCID iD for Walsh, Tiffany R. orcid.org/0000-0002-0233-9484
Noro, Massimo G.
Notman, Rebecca
Journal name PLoS one
Volume number 10
Issue number 7
Season Article Number : e0132706
Start page 1
End page 22
Total pages 22
Publisher PLoS
Place of publication San Francisco, Calif.
Publication date 2015-07-16
ISSN 1932-6203
Summary Keratins are cytoskeletal proteins that hierarchically arrange into filaments, starting with the dimer sub-unit. They are integral to the structural support of cells, in skin, hair and nails. In skin, keratin is thought to play a critical role in conferring the barrier properties and elasticity of skin. In general, the keratin dimer is broadly described by a tri-domain structure: a head, a central rod and a tail. As yet, no atomistic-scale picture of the entire dimer structure exists; this information is pivotal for establishing molecular-level connections between structure and function in intermediate filament proteins. The roles of the head and tail domains in facilitating keratin filament assembly and function remain as open questions. To address these, we report results of molecular dynamics simulations of the entire epithelial human K1/K10 keratin dimer. Our findings comprise: (1) the first three-dimensional structural models of the complete dimer unit, comprising of the head, rod and tail domains; (2) new insights into the chirality of the rod-domain twist gained from analysis of the full domain structure; (3) evidence for tri-subdomain partitioning in the head and tail domains; and, (4) identification of the residue characteristics that mediate non-covalent contact between the chains in the dimer. Our findings are immediately applicable to other epithelial keratins, such as K8/K18 and K5/K14, and to intermediate filament proteins in general.
Language eng
DOI 10.1371/journal.pone.0132706
Field of Research 030406 Proteins and Peptides
030402 Biomolecular Modelling and Design
030304 Physical Chemistry of Materials
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2015, The Authors
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30077503

Document type: Journal Article
Collections: Institute for Frontier Materials
Open Access Collection
GTP Research
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.