Convenient Desktop-scale Production of the Extracellular Domain of the Human Growth Hormone Receptor by an Insect-baculovirus Secretion System Using a Protein-free Culture

1995 ◽  
Vol 59 (10) ◽  
pp. 1976-1978 ◽  
Author(s):  
Akira Asakura ◽  
Mayumi Minami ◽  
Yoshimi Ota
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Human Growth ◽  
Extracellular Domain ◽  
Secretion System ◽  
Scale Production ◽  
Human Growth Hormone Receptor

Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule

Science ◽  
1991 ◽  
Vol 254 (5033) ◽  
pp. 821-825 ◽  
Author(s):  
B. Cunningham ◽  
M Ultsch ◽  
A. De Vos ◽  
M. Mulkerrin ◽  
K. Clauser ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Human Growth ◽  
Extracellular Domain ◽  
Human Growth Hormone Receptor

High-level secretion of the extracellular domain of the human growth hormone receptor using a baculovirus system

Gene ◽  
1991 ◽  
Vol 106 (2) ◽  
pp. 159-164 ◽  
Author(s):  
Ota Yoshimi ◽  
Asakura Akira ◽  
Matsuura Yoshiharu ◽  
Kendo Hidemasa ◽  
Hitoshio Akio ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Human Growth ◽  
Extracellular Domain ◽  
Baculovirus System ◽  
High Level ◽  
Human Growth Hormone Receptor

scholarly journals Order and disorder—An integrative structure of the full-length human growth hormone receptor

2021 ◽  
Vol 7 (27) ◽  
pp. eabh3805
Author(s):  
Noah Kassem ◽  
Raul Araya-Secchi ◽  
Katrine Bugge ◽  
Abigail Barclay ◽  
Helena Steinocher ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Lipid Membrane ◽  
Human Growth ◽  
Full Length ◽  
Saxs Data ◽  
X Ray ◽  
Human Growth Hormone Receptor

Because of its small size (70 kilodalton) and large content of structural disorder (>50%), the human growth hormone receptor (hGHR) falls between the cracks of conventional high-resolution structural biology methods. Here, we study the structure of the full-length hGHR in nanodiscs with small-angle x-ray scattering (SAXS) as the foundation. We develop an approach that combines SAXS, x-ray diffraction, and NMR spectroscopy data obtained on individual domains and integrate these through molecular dynamics simulations to interpret SAXS data on the full-length hGHR in nanodiscs. The hGHR domains reorient freely, resulting in a broad structural ensemble, emphasizing the need to take an ensemble view on signaling of relevance to disease states. The structure provides the first experimental model of any full-length cytokine receptor in a lipid membrane and exemplifies how integrating experimental data from several techniques computationally may access structures of membrane proteins with long, disordered regions, a widespread phenomenon in biology.

scholarly journals Mapping of a Cytoplasmic Domain of the Human Growth Hormone Receptor That Regulates Rates of Inactivation of Jak2 and Stat Proteins

1997 ◽  
Vol 272 (17) ◽  
pp. 11128-11132 ◽  
Author(s):  
Rebecca H. Hackett ◽  
Yi-Ding Wang ◽  
Sharon Sweitzer ◽  
Gerald Feldman ◽  
William I. Wood ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Human Growth ◽  
Cytoplasmic Domain ◽  
Stat Proteins ◽  
Human Growth Hormone Receptor

Expression of two isoforms of the human growth hormone receptor in normal liver and hepatocarcinoma

1994 ◽  
Vol 103 (1-2) ◽  
pp. 13-20 ◽  
Author(s):  
Nazario Esposito ◽  
Patricia Paterlini ◽  
Paul A. Kelly ◽  
Marie-Catherine Postel-Vinay ◽  
Joelle Finidori
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Human Growth ◽  
Normal Liver ◽  
Human Growth Hormone Receptor
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