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A conserved spider silk domain acts as a molecular switch that controls fibre assembly

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A conserved spider silk domain acts as a molecular switch that controls fibre assembly. / Hagn, Franz; Eisoldt, Lukas; Hardy, John G.; Vendrely, Charlotte; Coles, Murray; Scheibel, Thomas; Kessler, Horst.

In: Nature, Vol. 465, No. 7295, 13.05.2010, p. 239-242.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Hagn, F, Eisoldt, L, Hardy, JG, Vendrely, C, Coles, M, Scheibel, T & Kessler, H 2010, 'A conserved spider silk domain acts as a molecular switch that controls fibre assembly', Nature, vol. 465, no. 7295, pp. 239-242. https://doi.org/10.1038/nature08936

APA

Hagn, F., Eisoldt, L., Hardy, J. G., Vendrely, C., Coles, M., Scheibel, T., & Kessler, H. (2010). A conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature, 465(7295), 239-242. https://doi.org/10.1038/nature08936

Vancouver

Hagn F, Eisoldt L, Hardy JG, Vendrely C, Coles M, Scheibel T et al. A conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature. 2010 May 13;465(7295):239-242. https://doi.org/10.1038/nature08936

Author

Hagn, Franz ; Eisoldt, Lukas ; Hardy, John G. ; Vendrely, Charlotte ; Coles, Murray ; Scheibel, Thomas ; Kessler, Horst. / A conserved spider silk domain acts as a molecular switch that controls fibre assembly. In: Nature. 2010 ; Vol. 465, No. 7295. pp. 239-242.

Bibtex

@article{a43abb0fb7d34bb99f3df69b60c867cb,
title = "A conserved spider silk domain acts as a molecular switch that controls fibre assembly",
abstract = "A huge variety of proteins are able to form fibrillar structures(1), especially at high protein concentrations. Hence, it is surprising that spider silk proteins can be stored in a soluble form at high concentrations and transformed into extremely stable fibres on demand(2,3). Silk proteins are reminiscent of amphiphilic block copolymers containing stretches of polyalanine and glycine-rich polar elements forming a repetitive core flanked by highly conserved non-repetitive amino-terminal(4,5) and carboxy-terminal(6) domains. The N-terminal domain comprises a secretion signal, but further functions remain unassigned. The C-terminal domain was implicated in the control of solubility and fibre formation(7) initiated by changes in ionic composition(8,9) and mechanical stimuli known to align the repetitive sequence elements and promote beta-sheet formation(10-14). However, despite recent structural data(15), little is known about this remarkable behaviour in molecular detail. Here we present the solution structure of the C-terminal domain of a spider dragline silk protein and provide evidence that the structural state of this domain is essential for controlled switching between the storage and assembly forms of silk proteins. In addition, the C-terminal domain also has a role in the alignment of secondary structural features formed by the repetitive elements in the backbone of spider silk proteins, which is known to be important for the mechanical properties of the fibre.",
keywords = "TERMINAL DOMAIN, EXCHANGE-RATES, PROTEINS, DRAGLINE, ASSIGNMENT, STABILITY, MECHANISM, SEQUENCE, SHIFT, supramolecular chemistry, protein assembly, Biochemistry, Genetics and Molecular Biology(all), Biomaterials",
author = "Franz Hagn and Lukas Eisoldt and Hardy, {John G.} and Charlotte Vendrely and Murray Coles and Thomas Scheibel and Horst Kessler",
year = "2010",
month = may,
day = "13",
doi = "10.1038/nature08936",
language = "English",
volume = "465",
pages = "239--242",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "7295",

}

RIS

TY - JOUR

T1 - A conserved spider silk domain acts as a molecular switch that controls fibre assembly

AU - Hagn, Franz

AU - Eisoldt, Lukas

AU - Hardy, John G.

AU - Vendrely, Charlotte

AU - Coles, Murray

AU - Scheibel, Thomas

AU - Kessler, Horst

PY - 2010/5/13

Y1 - 2010/5/13

N2 - A huge variety of proteins are able to form fibrillar structures(1), especially at high protein concentrations. Hence, it is surprising that spider silk proteins can be stored in a soluble form at high concentrations and transformed into extremely stable fibres on demand(2,3). Silk proteins are reminiscent of amphiphilic block copolymers containing stretches of polyalanine and glycine-rich polar elements forming a repetitive core flanked by highly conserved non-repetitive amino-terminal(4,5) and carboxy-terminal(6) domains. The N-terminal domain comprises a secretion signal, but further functions remain unassigned. The C-terminal domain was implicated in the control of solubility and fibre formation(7) initiated by changes in ionic composition(8,9) and mechanical stimuli known to align the repetitive sequence elements and promote beta-sheet formation(10-14). However, despite recent structural data(15), little is known about this remarkable behaviour in molecular detail. Here we present the solution structure of the C-terminal domain of a spider dragline silk protein and provide evidence that the structural state of this domain is essential for controlled switching between the storage and assembly forms of silk proteins. In addition, the C-terminal domain also has a role in the alignment of secondary structural features formed by the repetitive elements in the backbone of spider silk proteins, which is known to be important for the mechanical properties of the fibre.

AB - A huge variety of proteins are able to form fibrillar structures(1), especially at high protein concentrations. Hence, it is surprising that spider silk proteins can be stored in a soluble form at high concentrations and transformed into extremely stable fibres on demand(2,3). Silk proteins are reminiscent of amphiphilic block copolymers containing stretches of polyalanine and glycine-rich polar elements forming a repetitive core flanked by highly conserved non-repetitive amino-terminal(4,5) and carboxy-terminal(6) domains. The N-terminal domain comprises a secretion signal, but further functions remain unassigned. The C-terminal domain was implicated in the control of solubility and fibre formation(7) initiated by changes in ionic composition(8,9) and mechanical stimuli known to align the repetitive sequence elements and promote beta-sheet formation(10-14). However, despite recent structural data(15), little is known about this remarkable behaviour in molecular detail. Here we present the solution structure of the C-terminal domain of a spider dragline silk protein and provide evidence that the structural state of this domain is essential for controlled switching between the storage and assembly forms of silk proteins. In addition, the C-terminal domain also has a role in the alignment of secondary structural features formed by the repetitive elements in the backbone of spider silk proteins, which is known to be important for the mechanical properties of the fibre.

KW - TERMINAL DOMAIN

KW - EXCHANGE-RATES

KW - PROTEINS

KW - DRAGLINE

KW - ASSIGNMENT

KW - STABILITY

KW - MECHANISM

KW - SEQUENCE

KW - SHIFT

KW - supramolecular chemistry

KW - protein assembly

KW - Biochemistry, Genetics and Molecular Biology(all)

KW - Biomaterials

U2 - 10.1038/nature08936

DO - 10.1038/nature08936

M3 - Journal article

VL - 465

SP - 239

EP - 242

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7295

ER -