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

Katrine Bugge; Elena Papaleo; Gitte W. Haxholm; Jonathan T. S. Hopper; Carol V. Robinson; Johan G. Olsen; Kresten Lindorff-Larsen; Birthe B. Kragelund

doi:10.1038/ncomms11578

Nature Communications (May 2016)

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

Katrine Bugge,
Elena Papaleo,
Gitte W. Haxholm,
Jonathan T. S. Hopper,
Carol V. Robinson,
Johan G. Olsen,
Kresten Lindorff-Larsen,
Birthe B. Kragelund

Affiliations

Katrine Bugge: Department of Biology, Structural Biology and NMR Laboratory, University of Copenhagen
Elena Papaleo: Department of Biology, Structural Biology and NMR Laboratory, University of Copenhagen
Gitte W. Haxholm: Department of Biology, Structural Biology and NMR Laboratory, University of Copenhagen
Jonathan T. S. Hopper: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
Carol V. Robinson: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
Johan G. Olsen: Department of Biology, Structural Biology and NMR Laboratory, University of Copenhagen
Kresten Lindorff-Larsen: Department of Biology, Structural Biology and NMR Laboratory, University of Copenhagen
Birthe B. Kragelund: Department of Biology, Structural Biology and NMR Laboratory, University of Copenhagen

DOI: https://doi.org/10.1038/ncomms11578
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 11

Abstract

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The prolactin receptor consists of a folded extracellular domain, a transmembrane domain and an intracellular intrinsically disordered domain. Here the authors use a combined experimental and computational approach to obtain a structure of a class I cytokine receptor, the human prolactin receptor.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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