Bray, David, Walsh, Tiffany R., Noro, Massimo G. and Notman, Rebecca (2015) Complete structure of an epithelial Keratin Dimer : implications for intermediate filament assembly. PLoS One, 10 (7). e0132706. doi:10.1371/journal.pone.0132706

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Abstract

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.

Item Type:	Journal Article
Subjects:	Q Science > QP Physiology
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Keratin, Cytoskeletal proteins, Intermediate filament proteins
Journal or Publication Title:	PLoS One
Publisher:	Public Library of Science
ISSN:	1932-6203
Official Date:	16 July 2015
Dates:	Date Event 16 July 2015 Published 17 June 2015 Accepted
Date of first compliant deposit:	9 January 2018
Volume:	10
Number:	7
Article Number:	e0132706
DOI:	10.1371/journal.pone.0132706
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Open Access
RIOXX Funder/Project Grant:	Project/Grant ID RIOXX Funder Name Funder ID UNSPECIFIED Unilever http://dx.doi.org/10.13039/100007190 Research Fellowship Royal Society http://dx.doi.org/10.13039/501100000288 UNSPECIFIED Veski (Firm) UNSPECIFIED

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