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Molecular Pharmacology

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Research ArticleArticle

A Hydrogen-Bonded Polar Network in the Core of the Glucagon-Like Peptide-1 Receptor is a Fulcrum for Biased Agonism: Lessons from Class B Crystal Structures.

Denise M. Wootten, Christopher A Reynolds, Cassandra Koole, Kevin J Smith, Juan C Mobarec, John Simms, Tezz Quon, Thomas Coudrat, Sebastian G.B. Furness, Laurence J Miller, Arthur Christopoulos and Patrick Sexton
Molecular Pharmacology December 23, 2015, mol.115.101246; DOI: https://doi.org/10.1124/mol.115.101246
Denise M. Wootten
1 Moansh University;
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Christopher A Reynolds
2 University of Essex;
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Cassandra Koole
3 Monash University;
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Kevin J Smith
2 University of Essex;
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Juan C Mobarec
2 University of Essex;
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John Simms
4 Aston University;
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Tezz Quon
3 Monash University;
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Thomas Coudrat
3 Monash University;
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Sebastian G.B. Furness
3 Monash University;
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Laurence J Miller
5 Mayo Clinic
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Arthur Christopoulos
3 Monash University;
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Patrick Sexton
3 Monash University;
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Data Supplement

Files in this Data Supplement:

  • Supplemental Data -

    Supplementary Figure 1 - Hydrogen bonds for the polar network residues of the GLP-1R apo inactive receptor during the 240 ns molecular dynamics simulation

  • Supplemental Table -

    ECL1 distance constraints and other constraints used in Modeller

  • GLP1R_full-length_GLP1 bound_G protein peptide bound.pdb -

    Full-length, peptide bound model of the human GLP-1 receptor

  • GLP1R apo.pdb -

    Inactive transmembrane domain model of the human GLP-1 receptor

  • Supplemental Movie -

    Close up of the polar network residues of GLP-1R during the molecular dynamics simulations

  View article

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