A combined computational and structural model of the full-length human prolactin receptor

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Standard

A combined computational and structural model of the full-length human prolactin receptor. / Bugge, Katrine Østergaard; Papaleo, Elena; Haxholm, Gitte Wolfsberg; Hopper, Jonathan T.S.; Robinson, Carol V.; Olsen, Johan Gotthardt; Lindorff-Larsen, Kresten; Kragelund, Birthe Brandt.

I: Nature Communications, Bind 7, 11578, 2016.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Bugge, KØ, Papaleo, E, Haxholm, GW, Hopper, JTS, Robinson, CV, Olsen, JG, Lindorff-Larsen, K & Kragelund, BB 2016, 'A combined computational and structural model of the full-length human prolactin receptor', Nature Communications, bind 7, 11578. https://doi.org/10.1038/ncomms11578

APA

Bugge, K. Ø., Papaleo, E., Haxholm, G. W., Hopper, J. T. S., Robinson, C. V., Olsen, J. G., Lindorff-Larsen, K., & Kragelund, B. B. (2016). A combined computational and structural model of the full-length human prolactin receptor. Nature Communications, 7, [11578]. https://doi.org/10.1038/ncomms11578

Vancouver

Bugge KØ, Papaleo E, Haxholm GW, Hopper JTS, Robinson CV, Olsen JG o.a. A combined computational and structural model of the full-length human prolactin receptor. Nature Communications. 2016;7. 11578. https://doi.org/10.1038/ncomms11578

Author

Bugge, Katrine Østergaard ; Papaleo, Elena ; Haxholm, Gitte Wolfsberg ; Hopper, Jonathan T.S. ; Robinson, Carol V. ; Olsen, Johan Gotthardt ; Lindorff-Larsen, Kresten ; Kragelund, Birthe Brandt. / A combined computational and structural model of the full-length human prolactin receptor. I: Nature Communications. 2016 ; Bind 7.

Bibtex

@article{996deb932eab4985aa5f7f8dc3eae495,
title = "A combined computational and structural model of the full-length human prolactin receptor",
abstract = "The prolactin receptor is an archetype member of the class I cytokine receptor family, comprising receptors with fundamental functions in biology as well as key drug targets. Structurally, each of these receptors represent an intriguing diversity, providing an exceptionally challenging target for structural biology. Here, we access the molecular architecture of the monomeric human prolactin receptor by combining experimental and computational efforts. We solve the NMR structure of its transmembrane domain in micelles and collect structural data on overlapping fragments of the receptor with small-angle X-ray scattering, native mass spectrometry and NMR spectroscopy. Along with previously published data, these are integrated by molecular modelling to generate a full receptor structure. The result provides the first full view of a class I cytokine receptor, exemplifying the architecture of more than 40 different receptor chains, and reveals that the extracellular domain is merely the tip of a molecular iceberg.",
author = "Bugge, {Katrine {\O}stergaard} and Elena Papaleo and Haxholm, {Gitte Wolfsberg} and Hopper, {Jonathan T.S.} and Robinson, {Carol V.} and Olsen, {Johan Gotthardt} and Kresten Lindorff-Larsen and Kragelund, {Birthe Brandt}",
year = "2016",
doi = "10.1038/ncomms11578",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - A combined computational and structural model of the full-length human prolactin receptor

AU - Bugge, Katrine Østergaard

AU - Papaleo, Elena

AU - Haxholm, Gitte Wolfsberg

AU - Hopper, Jonathan T.S.

AU - Robinson, Carol V.

AU - Olsen, Johan Gotthardt

AU - Lindorff-Larsen, Kresten

AU - Kragelund, Birthe Brandt

PY - 2016

Y1 - 2016

N2 - The prolactin receptor is an archetype member of the class I cytokine receptor family, comprising receptors with fundamental functions in biology as well as key drug targets. Structurally, each of these receptors represent an intriguing diversity, providing an exceptionally challenging target for structural biology. Here, we access the molecular architecture of the monomeric human prolactin receptor by combining experimental and computational efforts. We solve the NMR structure of its transmembrane domain in micelles and collect structural data on overlapping fragments of the receptor with small-angle X-ray scattering, native mass spectrometry and NMR spectroscopy. Along with previously published data, these are integrated by molecular modelling to generate a full receptor structure. The result provides the first full view of a class I cytokine receptor, exemplifying the architecture of more than 40 different receptor chains, and reveals that the extracellular domain is merely the tip of a molecular iceberg.

AB - The prolactin receptor is an archetype member of the class I cytokine receptor family, comprising receptors with fundamental functions in biology as well as key drug targets. Structurally, each of these receptors represent an intriguing diversity, providing an exceptionally challenging target for structural biology. Here, we access the molecular architecture of the monomeric human prolactin receptor by combining experimental and computational efforts. We solve the NMR structure of its transmembrane domain in micelles and collect structural data on overlapping fragments of the receptor with small-angle X-ray scattering, native mass spectrometry and NMR spectroscopy. Along with previously published data, these are integrated by molecular modelling to generate a full receptor structure. The result provides the first full view of a class I cytokine receptor, exemplifying the architecture of more than 40 different receptor chains, and reveals that the extracellular domain is merely the tip of a molecular iceberg.

U2 - 10.1038/ncomms11578

DO - 10.1038/ncomms11578

M3 - Journal article

C2 - 27174498

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 11578

ER -

ID: 161362912