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A Sequence Motif in the Transmembrane Region of Tyrosine Kinase Growth Factor Receptors

  • Michael J. E. Sternberg
  • William J. Gullick
Conference paper
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 7)

Abstract

The tyrosine kinase (TK) family of growth factor receptors (GFR) consists of one or more polypeptide chains organised into three regions; an N-terminal extracellular domain followed by a transmembrane section that leads to the intracellular domain e.g. (Hanks et al., 1988; Gullick, 1988). Ligand binding to the extracellular domain conveys the signal to the intracellular domain to induce its TK activity. This increase in TK activity then conveys the mitogenic stimulus to the nucleus promoting cell growth and division. The mechanism by which extracellular ligand binding stimulates intracellular TK activity is uncertain but there is considerable indirect evidence (e.g. Yarden and Schlessinger, 1987) that binding alters the conformation of the extracellular domain and promotes dimerisation of the receptors.

Keywords

Versus Versus Versus Transmembrane Region Tyrosine Kinase Growth Factor Receptor Small Side Chain Imperial Cancer Research Fund 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • Michael J. E. Sternberg
    • 1
  • William J. Gullick
    • 2
  1. 1.Biomolecular Modelling LaboratoryImperial Cancer Research FundLondonUK
  2. 2.Molecular Oncology Laboratory, Imperial Cancer Research Fund, Oncology GroupHammersmith HospitalLondonUK

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