Crystallization and preliminary x-ray diffraction analysis of the unliganded human growth hormone receptor

McKinstry, William J., Wan,Yu, Adams,Julian J., Brown, Richard J., Waters, Michael J. and Parker, Michael W. (2004) Crystallization and preliminary x-ray diffraction analysis of the unliganded human growth hormone receptor. Acta Crystallographica Section D: Biological Crystallography, 60 2380-2382. doi:10.1107/S090744490402757X

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Author McKinstry, William J.
Wan,Yu
Adams,Julian J.
Brown, Richard J.
Waters, Michael J.
Parker, Michael W.
Title Crystallization and preliminary x-ray diffraction analysis of the unliganded human growth hormone receptor
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
Publication date 2004
Sub-type Article (original research)
DOI 10.1107/S090744490402757X
Open Access Status File (Publisher version)
Volume 60
Start page 2380
End page 2382
Total pages 3
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell
Collection year 2004
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
730105 Endocrine organs and diseases (incl. diabetes)
Abstract The crystal structure of the extracellular domain of growth hormone receptor complexed to its ligand, growth hormone, has been known since 1992. However, no information exists for the unliganded form of the receptor. The human growth hormone receptor's extracellular ligand-binding domain, encompassing amino-acid residues 1 - 238, has been expressed in Escherichia coli, purified by anion ion-exchange chromatography and crystallized in its unliganded state by the hanging-drop vapour-diffusion method in 100 mM HEPES pH 7.0 containing 27.5%(w/v) PEG 5000 monomethyl ether and 200 mM ammonium sulfate as the co-precipitants. The crystals belong to the othorhombic space group C222(1), have unit-cell parameters a = 99.7, b = 112.2, c = 93.2 Angstrom and diffract to 2.5 Angstrom resolution using synchrotron radiation. The crystal structure will shed light on the nature of any conformation changes that occur upon ligand binding and will provide information to develop potential low-molecular-weight agonists/antagonists to treat clinical diseases in which the growth hormone receptor is implicated.
Keyword Biochemical Research Methods
Biochemistry & Molecular Biology
Biophysics
Crystallography
Extracellular Domain
Dimerization
Binding
Design
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 04:45:57 EST