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Comparative Analysis of Human Growth Hormone in Serum Using SPRi, Nano-SPRi and ELISA Assays
11:17

Comparative Analysis of Human Growth Hormone in Serum Using SPRi, Nano-SPRi and ELISA Assays

Published on: January 7, 2016

Growth hormone receptor: structure function relationships.

Michael J Waters1, Andrew J Brooks

  • 1Institute for Molecular Bioscience, University of Queensland, St. Lucia, Qld., Australia. m.waters @ imb.uq.eddu.au

Hormone Research in Paediatrics
|July 23, 2011
PubMed
Summary
This summary is machine-generated.

The growth hormone receptor (GHR) dimerizes constitutively, with activation triggered by conformational changes. This structural plasticity allows differential kinase activation by growth hormone (GH) analogues.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Cell Signaling

Background:

  • The growth hormone receptor (GHR), a class 1 cytokine receptor, has been extensively studied, with solved crystal structures revealing binding sites for growth hormone (GH).
  • GHR activation was traditionally attributed to hormone-induced dimerization, but evidence suggests a pre-formed dimer activated by conformational shifts.
  • Two distinct tyrosine kinases, Janus kinase 2 (JAK2) and an Src-family kinase, associate with GHR, mediating different downstream signaling pathways.

Discussion:

  • The GHR transmembrane domain (TMD) interactions are crucial for receptor dimerization and subsequent activation.
  • Hormone binding induces conformational changes, including subunit rotation and scissor movements, essential for JAK2 activation.
  • Src-family kinase activation involves a distinct conformational change in the lower sandwich module and a different TMD orientation compared to JAK2 activation.

Key Insights:

  • GHR exists as a constitutive dimer, challenging the long-held view of hormone-induced dimerization as the sole activation mechanism.
  • Differential activation of JAK2 and Src-family kinases is mediated by distinct conformational states of the GHR.
  • Structural plasticity within the GHR, particularly in the TMD and lower sandwich module, dictates kinase recruitment and activation.

Outlook:

  • The structural differences in GHR activation pathways offer opportunities for developing targeted GH analogues, such as I179M human GH.
  • Understanding these distinct activation mechanisms can lead to novel therapeutic strategies for conditions related to growth hormone signaling.
  • Further structural and biochemical studies will elucidate the precise molecular events governing differential kinase activation by GHR.