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Science 8 November 1991:
Vol. 254. no. 5033, pp. 821 - 825
DOI: 10.1126/science.1948064
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Articles

Science, Vol 254, Issue 5033, 821-825
Copyright © 1991 by American Association for the Advancement of Science

articles

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

BC Cunningham, M Ultsch, AM De Vos, MG Mulkerrin, KR Clauser, and JA Wells

Department of Protein Engineering, Genentech, Inc., South San Francisco, CA 94080.

Human growth hormone (hGH) forms a 1:2 complex with the extracellular domain of its receptor-binding protein (hGHbp) as studied by crystallization, size exclusion chromatography, calorimetry, and a previously undescribed fluorescence quenching assay. These and other experiments with protein engineered variants of hGH have led to the identification of the binding determinants for two distinct but adjacent sites on hGH for the hGHbp, and the data indicated that there are two overlapping binding sites on the hGHbp for hGH. Furthermore, the binding of hGH to the hGHbp occurred sequentially; a first hGHbp molecule bound to site 1 on hGH and then a second hGHbp bound to site 2. Hormone-induced receptor dimerization is proposed to be relevant to the signal transduction mechanism for the hGH receptor and other related cytokine receptors.


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Characteristics of circulating growth hormone in women after acute heavy resistance exercise.
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R. J. M. Ross, K. C. Leung, M. Maamra, W. Bennett, N. Doyle, M. J. Waters, and K. K. Y. Ho (2001)
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X Shi, S Amindari, K Paruchuru, D Skalla, H Burkin, B. Shur, and D. Miller (2001)
Development 128, 645-654
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Methods in Determining Growth Hormone Concentrations: An Immunofunctional Assay.
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P. Tollet-Egnell, A. Flores-Morales, A. Stavréus-Evers, L. Sahlin, and G. Norstedt (1999)
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J. Biol. Chem. 274, 5755-5761
   Abstract »    Full Text »    PDF »
Functional domains of human growth hormone necessary for the adipogenic activity of hGH/hPL chimeric molecules.
E Juarez-Aguilar, F Castro-Munozledo, N. Guerra-Rodriguez, D Resendez-Perez, H. Martinez-Rodriguez, H. Barrera-Saldana, and W Kuri-Harcuch (1999)
J. Cell Sci. 112, 3127-3135
   Abstract »    PDF »
Termination of Growth Hormone Pulse-Induced STAT5b Signaling.
C. A. Gebert, S.-H. Park, and D. J. Waxman (1999)
Mol. Endocrinol. 13, 38-56
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Four Contiguous Amino Acid Substitutions, Identified in Patients with Laron Syndrome, Differently Affect the Binding Affinity and Intracellular Trafficking of the Growth Hormone Receptor.
J. Wojcik, M. A. Berg, N. Esposito, M. E. Geffner, N. Sakati, E. O. Reiter, S. Dower, U. Francke, M.-C. Postel-Vinay, and J. Finidori (1998)
J. Clin. Endocrinol. Metab. 83, 4481-4489
   Abstract »    Full Text »
Interaction affinity between cytokine receptor components on the cell surface.
A. Whitty, N. Raskin, D. L. Olson, C. W. Borysenko, C. M. Ambrose, C. D. Benjamin, and L. C. Burkly (1998)
PNAS 95, 13165-13170
   Abstract »    Full Text »    PDF »
Interactions between scatter factors and their receptors: hints for therapeutic applications.
L. Trusolino, L. Pugliese, and P. M. Comoglio (1998)
FASEB J 12, 1267-1280
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Heparan Sulfate Oligosaccharides Require 6-O-Sulfation for Promotion of Basic Fibroblast Growth Factor Mitogenic Activity.
D. A. Pye, R. R. Vives, J. E. Turnbull, P. Hyde, and J. T. Gallagher (1998)
J. Biol. Chem. 273, 22936-22942
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Herpes Simplex Virus Glycoprotein D Can Bind to Poliovirus Receptor-Related Protein 1 or Herpesvirus Entry Mediator, Two Structurally Unrelated Mediators of Virus Entry.
C. Krummenacher, A. V. Nicola, J. C. Whitbeck, H. Lou, W. Hou, J. D. Lambris, R. J. Geraghty, P. G. Spear, G. H. Cohen, and R. J. Eisenberg (1998)
J. Virol. 72, 7064-7074