biostudies-literatureVoorhees JLNIDDK NIH HHS1783-8https://www.ebi.ac.uk/biostudies/studies/S-EPMC4648361biostudies-literatureUnknown585(12)Zinc half sites are present in all human lactogenic hormones: human prolactin (hPRL), growth hormone (hGH), placental lactogens (hPL) and the hPRL receptor (hPRLr). The influence of divalent zinc (Zn(2+)) as measured by intrinsic fluorescence or FRET in each of these hormones is unique and is affected by the presence of varying stoichiometries of hPRLr. These data show that both Zn(2+) and hPRLr binding influence hPRL conformers in an interdependent fashion. Although each of these three lactogenic hormones bind hPRLr and induce a biological response that is sensitive to the presence of increasing concentrations of Zn(2+), each hormone is unique in the mechanistic details of this process.FEBS lettersZinc binding to human lactogenic hormones and the human prolactin receptor.PMC4648361R01 DK072275DK-72245Brooks CLVoorhees JLRao GVGordon TJfalseZinc binding to human lactogenic hormones and the human prolactin receptor.Zinc half sites are present in all human lactogenic hormones: human prolactin (hPRL), growth hormone (hGH), placental lactogens (hPL) and the hPRL receptor (hPRLr). The influence of divalent zinc (Zn(2+)) as measured by intrinsic fluorescence or FRET in each of these hormones is unique and is affected by the presence of varying stoichiometries of hPRLr. These data show that both Zn(2+) and hPRLr binding influence hPRL conformers in an interdependent fashion. Although each of these three lactogenic hormones bind hPRLr and induce a biological response that is sensitive to the presence of increasing concentrations of Zn(2+), each hormone is unique in the mechanistic details of this process.2011-01-01T00:00:00Z2011 Jun2020-10-29T13:03:07Z2019-03-27T02:02:07ZS-EPMC46483612151094510.1016/j.febslet.2011.04.019