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Measurement of the formation of complexes in 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 fr...
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2007
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2483503/ https://www.ncbi.nlm.nih.gov/pubmed/17164523 http://dx.doi.org/10.1107/S0907444906046373 |
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author | Ladbury, John E. |
author_facet | Ladbury, John E. |
author_sort | Ladbury, John E. |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2483503 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-24835032009-03-05 Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction Ladbury, John E. Acta Crystallogr D Biol Crystallogr Research Papers 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. International Union of Crystallography 2007-01-01 2006-12-13 /pmc/articles/PMC2483503/ /pubmed/17164523 http://dx.doi.org/10.1107/S0907444906046373 Text en © International Union of Crystallography 2007 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html. |
spellingShingle | Research Papers Ladbury, John E. Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction |
title | Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction |
title_full | Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction |
title_fullStr | Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction |
title_full_unstemmed | Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction |
title_short | Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction |
title_sort | measurement of the formation of complexes in tyrosine kinase-mediated signal transduction |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2483503/ https://www.ncbi.nlm.nih.gov/pubmed/17164523 http://dx.doi.org/10.1107/S0907444906046373 |
work_keys_str_mv | AT ladburyjohne measurementoftheformationofcomplexesintyrosinekinasemediatedsignaltransduction |