Mapping the interaction between phosphorylated human growth hormone-growth hormone receptor using hydrogen/deuterium exchange mass spectrometry.

摘要

The interfacial region between the human growth hormone (hGH) and human growth hormone receptor (hGHR) is very well characterized by X-ray crystallographic studies. The GHR undergoes dimerization and conformational change upon binding to GH forming GH(GHR)2 complex. The role of GHR is to activate the Jak 2 kinase to initiate pathways, which ultimately end with the expression of insulin growth factor-1. However the role phosphorylation on receptor binding and signaling activation is not yet clear. In order to understand this aspect, we studied the interaction between phosphorylated hGH and hGHR. This task was accomplished by mapping the phosphorylated hGH-hGHR interfacial regions using hydrogen/deuterium exchange (HDX) and mass spectrometry (MS).