Transduction of biochemical signals across cell membranes

  title={Transduction of biochemical signals across cell membranes},
  author={Wayne A. Hendrickson},
  journal={Quarterly Reviews of Biophysics},
  pages={321 - 330}
  • W. Hendrickson
  • Published 1 November 2005
  • Biology
  • Quarterly Reviews of Biophysics
1. Introduction 321 2. Tyrosine kinase receptors 322 3. Histidine kinase sensors 325 4. G-protein coupled receptors 327 5. Principles 328 6. Acknowledgments 329 7. References 330 Biological cells need to be responsive to various stimuli, primarily chemical ligands from their environments. Specific receptor molecules embedded in the plasma membrane detect the different biochemical signals that impact the cell, and these receptors are the conduits for transmission of this information to the cell… 
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The author’s home country, the United States, and some of the authors’ relatives, have contributed to this work through the years.


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Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural
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Molecular basis of transmembrane signalling by sensory rhodopsin II–transducer complex
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Interaction between proteins localized in membranes.
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The Ants Go Marching Two by Two: Oligomeric Structure of G-Protein-Coupled Receptors
Experimental evidence supports the hypothesis that class A receptors may exist as higher-order oligomers, or even as arrays, with distinct symmetrical interfaces in both the first and fourth transmembrane segments.
Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
Comparisons with other kinase structures indicate that tyrosine phophophorylation and ligand binding may in general elicit two distinct hinge-like movements between the kinase subdomains, and a basis for inhibition by phosphorylation at Tyr 505 is suggested.
Structural interactions of fibroblast growth factor receptor with its ligands.
The crystal structure, determined by multiwavelength anomalous diffraction analysis of the selenomethionyl protein, is a dimeric assemblage of 1:1 ligand:receptor complexes that provides a structural mechanism for FGF signal transduction.
Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
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