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Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator

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Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator. / Sluchanko, Nikolai N; Beelen, Steven; Kulikova, Alexandra A; Weeks, Stephen D; Antson, Alfred A; Gusev, Nikolai B; Strelkov, Sergei V.

In: Structure, Vol. 25, No. 2, 07.02.2017, p. 305–316.

Research output: Contribution to journalArticle

Harvard

Sluchanko, NN, Beelen, S, Kulikova, AA, Weeks, SD, Antson, AA, Gusev, NB & Strelkov, SV 2017, 'Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator', Structure, vol. 25, no. 2, pp. 305–316. https://doi.org/10.1016/j.str.2016.12.005

APA

Sluchanko, N. N., Beelen, S., Kulikova, A. A., Weeks, S. D., Antson, A. A., Gusev, N. B., & Strelkov, S. V. (2017). Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator. Structure, 25(2), 305–316. https://doi.org/10.1016/j.str.2016.12.005

Vancouver

Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB et al. Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator. Structure. 2017 Feb 7;25(2):305–316. https://doi.org/10.1016/j.str.2016.12.005

Author

Sluchanko, Nikolai N ; Beelen, Steven ; Kulikova, Alexandra A ; Weeks, Stephen D ; Antson, Alfred A ; Gusev, Nikolai B ; Strelkov, Sergei V. / Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator. In: Structure. 2017 ; Vol. 25, No. 2. pp. 305–316.

Bibtex - Download

@article{a27454f8e14f4d80820a27bc300f45b5,
title = "Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator",
abstract = "By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6, within its intrinsically disordered N-terminal domain activates its interaction with 14-3-3, ultimately triggering smooth muscle relaxation. After analyzing the binding of an HSPB6-derived phosphopeptide to 14-3-3 using isothermal calorimetry and X-ray crystallography, we have determined the crystal structure of the complete assembly consisting of the 14-3-3 dimer and full-length HSPB6 dimer and further characterized this complex in solution using fluorescence spectroscopy, small-angle X-ray scattering, and limited proteolysis. We show that selected intrinsically disordered regions of HSPB6 are transformed into well-defined conformations upon the interaction, whereby an unexpectedly asymmetric structure is formed. This structure provides the first atomic resolution snapshot of a human small HSP in functional state, explains how 14-3-3 proteins sequester their regulatory partners, and can inform the design of small-molecule interaction modifiers to be used as myorelaxants.",
author = "Sluchanko, {Nikolai N} and Steven Beelen and Kulikova, {Alexandra A} and Weeks, {Stephen D} and Antson, {Alfred A} and Gusev, {Nikolai B} and Strelkov, {Sergei V}",
note = " {\textcopyright} 2017 Elsevier B.V. This is an author-produced version of the published paper. Uploaded in accordance with the publisher{\textquoteright}s self-archiving policy. Further copying may not be permitted; contact the publisher for details.",
year = "2017",
month = feb,
day = "7",
doi = "10.1016/j.str.2016.12.005",
language = "English",
volume = "25",
pages = "305–316",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "2",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator

AU - Sluchanko, Nikolai N

AU - Beelen, Steven

AU - Kulikova, Alexandra A

AU - Weeks, Stephen D

AU - Antson, Alfred A

AU - Gusev, Nikolai B

AU - Strelkov, Sergei V

N1 - © 2017 Elsevier B.V. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

PY - 2017/2/7

Y1 - 2017/2/7

N2 - By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6, within its intrinsically disordered N-terminal domain activates its interaction with 14-3-3, ultimately triggering smooth muscle relaxation. After analyzing the binding of an HSPB6-derived phosphopeptide to 14-3-3 using isothermal calorimetry and X-ray crystallography, we have determined the crystal structure of the complete assembly consisting of the 14-3-3 dimer and full-length HSPB6 dimer and further characterized this complex in solution using fluorescence spectroscopy, small-angle X-ray scattering, and limited proteolysis. We show that selected intrinsically disordered regions of HSPB6 are transformed into well-defined conformations upon the interaction, whereby an unexpectedly asymmetric structure is formed. This structure provides the first atomic resolution snapshot of a human small HSP in functional state, explains how 14-3-3 proteins sequester their regulatory partners, and can inform the design of small-molecule interaction modifiers to be used as myorelaxants.

AB - By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6, within its intrinsically disordered N-terminal domain activates its interaction with 14-3-3, ultimately triggering smooth muscle relaxation. After analyzing the binding of an HSPB6-derived phosphopeptide to 14-3-3 using isothermal calorimetry and X-ray crystallography, we have determined the crystal structure of the complete assembly consisting of the 14-3-3 dimer and full-length HSPB6 dimer and further characterized this complex in solution using fluorescence spectroscopy, small-angle X-ray scattering, and limited proteolysis. We show that selected intrinsically disordered regions of HSPB6 are transformed into well-defined conformations upon the interaction, whereby an unexpectedly asymmetric structure is formed. This structure provides the first atomic resolution snapshot of a human small HSP in functional state, explains how 14-3-3 proteins sequester their regulatory partners, and can inform the design of small-molecule interaction modifiers to be used as myorelaxants.

U2 - 10.1016/j.str.2016.12.005

DO - 10.1016/j.str.2016.12.005

M3 - Article

C2 - 28089448

VL - 25

SP - 305

EP - 316

JO - Structure

JF - Structure

SN - 0969-2126

IS - 2

ER -