skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction

Abstract

The use of isothermal titration calorimetry (ITC) provides a full thermodynamic characterization of an interaction in one experiment. The determination of the affinity is an important value; however, the additional layer of information provided by the change in enthalpy and entropy can help in understanding the biology. This is demonstrated with respect to tyrosine kinase-mediated signal transduction. Isothermal titration calorimetry (ITC) provides highly complementary data to high-resolution structural detail. An overview of the methodology of the technique is provided. Ultimately, the correlation of the thermodynamic parameters determined by ITC with structural perturbation observed on going from the free to the bound state should be possible at an atomic level. Currently, thermodynamic data provide some insight as to potential changes occurring on complex formation. Here, this is demonstrated in the context of in vitro quantification of intracellular tyrosine kinase-mediated signal transduction and the issue of specificity of the important interactions. The apparent lack of specificity in the interactions of domains of proteins involved in early signalling from membrane-bound receptors is demonstrated using data from ITC.

Authors:
 [1]
  1. Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT (United Kingdom)
Publication Date:
OSTI Identifier:
22347986
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 63; Journal Issue: Pt 1; Other Information: PMCID: PMC2483503; PUBLISHER-ID: ba5094; PMID: 17164523; OAI: oai:pubmedcentral.nih.gov:2483503; Copyright (c) International Union of Crystallography 2007; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AFFINITY; ATOMS; BOUND STATE; CALORIMETRY; CORRELATIONS; DISTURBANCES; ENTROPY; IN VITRO; INTERACTIONS; LAYERS; POTENTIALS; RECEPTORS; SIGNALS; SPECIFICITY

Citation Formats

Ladbury, John E., E-mail: j.ladbury@biochem.ucl.ac.uk. Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction. Denmark: N. p., 2007. Web. doi:10.1107/S0907444906046373.
Ladbury, John E., E-mail: j.ladbury@biochem.ucl.ac.uk. Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction. Denmark. doi:10.1107/S0907444906046373.
Ladbury, John E., E-mail: j.ladbury@biochem.ucl.ac.uk. Mon . "Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction". Denmark. doi:10.1107/S0907444906046373.
@article{osti_22347986,
title = {Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction},
author = {Ladbury, John E., E-mail: j.ladbury@biochem.ucl.ac.uk},
abstractNote = {The use of isothermal titration calorimetry (ITC) provides a full thermodynamic characterization of an interaction in one experiment. The determination of the affinity is an important value; however, the additional layer of information provided by the change in enthalpy and entropy can help in understanding the biology. This is demonstrated with respect to tyrosine kinase-mediated signal transduction. Isothermal titration calorimetry (ITC) provides highly complementary data to high-resolution structural detail. An overview of the methodology of the technique is provided. Ultimately, the correlation of the thermodynamic parameters determined by ITC with structural perturbation observed on going from the free to the bound state should be possible at an atomic level. Currently, thermodynamic data provide some insight as to potential changes occurring on complex formation. Here, this is demonstrated in the context of in vitro quantification of intracellular tyrosine kinase-mediated signal transduction and the issue of specificity of the important interactions. The apparent lack of specificity in the interactions of domains of proteins involved in early signalling from membrane-bound receptors is demonstrated using data from ITC.},
doi = {10.1107/S0907444906046373},
journal = {Acta Crystallographica. Section D: Biological Crystallography},
number = Pt 1,
volume = 63,
place = {Denmark},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}