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A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors

Research output: Contribution to journalArticlepeer-review

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A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors. / Saleh, Noureldin; Saladino, Giorgio; Gervasio, Francesco L.; Haensele, Elke; Banting, Lee; Whitley, David C.; Sopkova-de Oliveira Santos, Jana; Bureau, Ronan; Clark, Timothy.

In: Angewandte Chemie, Vol. 128, No. 28, 05.07.2016, p. 8140-8144.

Research output: Contribution to journalArticlepeer-review

Harvard

Saleh, N, Saladino, G, Gervasio, FL, Haensele, E, Banting, L, Whitley, DC, Sopkova-de Oliveira Santos, J, Bureau, R & Clark, T 2016, 'A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors', Angewandte Chemie, vol. 128, no. 28, pp. 8140-8144. https://doi.org/10.1002/ange.201602729

APA

Saleh, N., Saladino, G., Gervasio, F. L., Haensele, E., Banting, L., Whitley, D. C., Sopkova-de Oliveira Santos, J., Bureau, R., & Clark, T. (2016). A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors. Angewandte Chemie, 128(28), 8140-8144. https://doi.org/10.1002/ange.201602729

Vancouver

Saleh N, Saladino G, Gervasio FL, Haensele E, Banting L, Whitley DC et al. A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors. Angewandte Chemie. 2016 Jul 5;128(28):8140-8144. https://doi.org/10.1002/ange.201602729

Author

Saleh, Noureldin ; Saladino, Giorgio ; Gervasio, Francesco L. ; Haensele, Elke ; Banting, Lee ; Whitley, David C. ; Sopkova-de Oliveira Santos, Jana ; Bureau, Ronan ; Clark, Timothy. / A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors. In: Angewandte Chemie. 2016 ; Vol. 128, No. 28. pp. 8140-8144.

Bibtex

@article{3b53c1b2aabb48df91bb05a63b16b267,
title = "A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors",
abstract = "Molecular-dynamics simulations with metadynamics enhanced sampling reveal three distinct binding sites for arginine vasopressin (AVP) within its V2-receptor (V2R). Two of these, the vestibule and intermediate sites, block (antagonize) the receptor, and the third is the orthosteric activation (agonist) site. The contacts found for the orthosteric site satisfy all the requirements deduced from mutagenesis experiments. Metadynamics simulations for V2R and its V1aR-analog give an excellent correlation with experimental binding free energies by assuming that the most stable binding site in the simulations corresponds to the experimental binding free energy in each case. The resulting three-site mechanism separates agonists from antagonists and explains subtype selectivity.",
keywords = "uploaded-in-3-months-elsewhere",
author = "Noureldin Saleh and Giorgio Saladino and Gervasio, {Francesco L.} and Elke Haensele and Lee Banting and Whitley, {David C.} and Jana Sopkova-de Oliveira Santos and Ronan Bureau and Timothy Clark",
year = "2016",
month = jul,
day = "5",
doi = "10.1002/ange.201602729",
language = "English",
volume = "128",
pages = "8140--8144",
journal = "Angewandte Chemie",
issn = "0044-8249",
publisher = "Wiley",
number = "28",

}

RIS

TY - JOUR

T1 - A three-site mechanism for agonist/antagonist selective binding to vasopressin receptors

AU - Saleh, Noureldin

AU - Saladino, Giorgio

AU - Gervasio, Francesco L.

AU - Haensele, Elke

AU - Banting, Lee

AU - Whitley, David C.

AU - Sopkova-de Oliveira Santos, Jana

AU - Bureau, Ronan

AU - Clark, Timothy

PY - 2016/7/5

Y1 - 2016/7/5

N2 - Molecular-dynamics simulations with metadynamics enhanced sampling reveal three distinct binding sites for arginine vasopressin (AVP) within its V2-receptor (V2R). Two of these, the vestibule and intermediate sites, block (antagonize) the receptor, and the third is the orthosteric activation (agonist) site. The contacts found for the orthosteric site satisfy all the requirements deduced from mutagenesis experiments. Metadynamics simulations for V2R and its V1aR-analog give an excellent correlation with experimental binding free energies by assuming that the most stable binding site in the simulations corresponds to the experimental binding free energy in each case. The resulting three-site mechanism separates agonists from antagonists and explains subtype selectivity.

AB - Molecular-dynamics simulations with metadynamics enhanced sampling reveal three distinct binding sites for arginine vasopressin (AVP) within its V2-receptor (V2R). Two of these, the vestibule and intermediate sites, block (antagonize) the receptor, and the third is the orthosteric activation (agonist) site. The contacts found for the orthosteric site satisfy all the requirements deduced from mutagenesis experiments. Metadynamics simulations for V2R and its V1aR-analog give an excellent correlation with experimental binding free energies by assuming that the most stable binding site in the simulations corresponds to the experimental binding free energy in each case. The resulting three-site mechanism separates agonists from antagonists and explains subtype selectivity.

KW - uploaded-in-3-months-elsewhere

UR - http://discovery.ucl.ac.uk/10048283

U2 - 10.1002/ange.201602729

DO - 10.1002/ange.201602729

M3 - Article

VL - 128

SP - 8140

EP - 8144

JO - Angewandte Chemie

JF - Angewandte Chemie

SN - 0044-8249

IS - 28

ER -

ID: 4696957