ReviewProceedings of the National Academy of Sciences of the United States of America1996
Binding in the growth hormone receptor complex.
Review in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
87 citing papers in PubMed, 437 citations in OpenAlex.
- Sex-specific circadian and behavioral phenotypes in aged growth hormone receptor knockout mice.GeroScience · 2026Article
- Prolactin Regulates Ovine Ovarian Granulosa Cell Apoptosis by Affecting the Expression ofInternational journal of molecular sciences · 2023Article
- SOCS2 regulation of growth hormone signaling requires a canonical interaction with phosphotyrosine.Bioscience reports · 2022Article
- Dimeric mimetic of BDNF loop 4 promotes survival of serum-deprived cell through TrkB-dependent apoptosis suppression.Scientific reports · 2021Article
- The Role of Growth Hormone in Mesenchymal Stem Cell Commitment.International journal of molecular sciences · 2019Review
- FcαRI binding at the IgA1 CProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Growth Hormone Receptor Mutations Related to Individual Dwarfism.International journal of molecular sciences · 2018Review
- The Growth Hormone Receptor: Mechanism of Receptor Activation, Cell Signaling, and Physiological Aspects.Frontiers in endocrinology · 2018Review
- Self-assembled α-Tocopherol Transfer Protein Nanoparticles Promote Vitamin E Delivery Across an Endothelial Barrier.Scientific reports · 2017Article
- IL-7 Induces an Epitope Masking ofMediators of inflammation · 2017Article
- Saturation scanning of ubiquitin variants reveals a common hot spot for binding to USP2 and USP21.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Pressuromodulation at the cell membrane as the basis for small molecule hormone and peptide regulation of cellular and nuclear function.Journal of translational medicine · 2015Article
- Allosteric Dynamic Control of Binding.Biophysical journal · 2015Article
- Small-molecule inhibitors of the Myc oncoprotein.Biochimica et biophysica acta · 2015Review
- JAK2 activation by growth hormone and other cytokines.The Biochemical journal · 2015Review
- Structural basis for the recognition of human cytomegalovirus glycoprotein B by a neutralizing human antibody.PLoS pathogens · 2014Article
- Article
- Conformational instability of human prion protein upon residue modification: a molecular dynamics simulation study.EXCLI journal · 2014Article
- Crystal structures of interleukin 17A and its complex with IL-17 receptor A.Nature communications · 2013Article
- Growth hormone variants: a potential avenue for a better diagnostic characterization of growth hormone deficiency in children.Journal of endocrinological investigation · 2012Review
27 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Binding reactions between human growth hormone (hGH) and its receptor provide a detailed account of how a polypeptide hormone activates its receptor and more generally how proteins interact. Through high-resolution structural and functional studies it is seen that hGH uses two different sites (site 1 and site 2) to bind two identical receptor molecules. This sequential dimerization reaction activates the receptor, presumably by bringing the intracellular domains into close proximity so they may activate cytosolic components. As a consequence of this mechanism it is possible to build antagonists to the receptor by introducing mutations in hGH that block binding at site 2 and to build even more potent antagonists by combining these with mutants that enhance binding at site 1. Alanine-scanning mutagenesis of all contact residues at the site 1 interface shows that only a small and complementary set of side chains clustered near the center of the interface affects binding. The most important contacts are hydrophobic, and these are surrounded by polar and charged interactions of lesser importance. Kinetic analysis shows for the most part that the important side chains function to maintain the complex, not to guide the hormone to the receptor. Hormone-induced homodimerization or heterodimerization reactions are turning out to be pervasive mechanisms for signal transduction. Moreover, the molecular recognition principles seen in the hGH-receptor complex are likely to generalize to other protein-protein complexes.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.