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Groothuizen FS, Poger D, Mark AE. Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain. J Chem Theory Comput. 2010;6(10):3274-83doi: 10.1021/ct1003934.
Groothuizen, F. S., Poger, D., & Mark, A. E. (2010). Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain. Journal of chemical theory and computation, 6(10), 3274-83. https://doi.org/10.1021/ct1003934
Groothuizen, Flora S, et al. "Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain." Journal of chemical theory and computation vol. 6,10 (2010): 3274-83. doi: https://doi.org/10.1021/ct1003934
Groothuizen FS, Poger D, Mark AE. Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain. J Chem Theory Comput. 2010 Oct 12;6(10):3274-83. doi: 10.1021/ct1003934. PMID: 26616789.
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J Chem Theory Comput. 2010 Oct 12;6(10):3274-83. doi: 10.1021/ct1003934.

Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain.

Journal of chemical theory and computation

Flora S Groothuizen, David Poger, Alan E Mark

Affiliations

  1. School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia, and Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.

PMID: 26616789 DOI: 10.1021/ct1003934

Abstract

The prolactin receptor resides on the surface of the cell as a preformed dimer. This suggests that cell signaling is triggered by conformational changes within the extracellular domain of the receptors. Here, by using atomistic molecular dynamics simulations, we show that the removal of the ligand placental lactogen from the dimeric form of the prolactin receptor results in a relative reorientation of the two extracellular domains by 20-30°, which corresponds to a clockwise rotation of the domains with respect to each other. Such a mechanism of activation for the prolactin receptor is similar to that proposed previously in the case of the growth hormone receptor. In addition to the effect of the removal of the ligand, the mechanical coupling between the extracellular and transmembrane domains within a model membrane was also examined.

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