Allosteric cooperativity in protein kinase A

by: Larry R Masterson, Alessandro Mascioni, Nathaniel J Traaseth, Susan S Taylor, Gianluigi Veglia

Proceedings of the National Academy of Sciences, Vol. 105, No. 2. (15 January 2008), pp. 506-511.

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Abstract

Allosteric signaling in proteins requires long-range communication mediated by highly conserved residues, often triggered by ligand binding. In this article, we map the allosteric network in the catalytic subunit of protein kinase A using NMR spectroscopy. We show that positive allosteric cooperativity is generated by nucleotide and substrate binding during the transitions through the major conformational states: apo, intermediate, and closed. The allosteric network is disrupted by a single site mutation (Y204A), which also decouples the cooperativity of ligand binding. Because protein kinase A is the prototype for the entire kinome, these findings may serve as a paradigm for describing long-range coupling in other protein kinases. 10.1073/pnas.0709214104

@article{citeulike:2368518, abstract = {Allosteric signaling in proteins requires long-range communication mediated by highly conserved residues, often triggered by ligand binding. In this article, we map the allosteric network in the catalytic subunit of protein kinase A using NMR spectroscopy. We show that positive allosteric cooperativity is generated by nucleotide and substrate binding during the transitions through the major conformational states: apo, intermediate, and closed. The allosteric network is disrupted by a single site mutation (Y204A), which also decouples the cooperativity of ligand binding. Because protein kinase A is the prototype for the entire kinome, these findings may serve as a paradigm for describing long-range coupling in other protein kinases. 10.1073/pnas.0709214104}, author = {Masterson, Larry R. and Mascioni, Alessandro and Traaseth, Nathaniel J. and Taylor, Susan S. and Veglia, Gianluigi }, citeulike-article-id = {2368518}, doi = {10.1073/pnas.0709214104}, journal = {Proceedings of the National Academy of Sciences}, keywords = {allostery, experiment, nmr}, month = {January}, number = {2}, pages = {506--511}, posted-at = {2008-02-13 06:23:34}, priority = {2}, title = {Allosteric cooperativity in protein kinase A}, url = {http://dx.doi.org/10.1073/pnas.0709214104}, volume = {105}, year = {2008} }

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TY - JOUR ID - citeulike:2368518 L3 - citeulike-article-id:2368518 TI - Allosteric cooperativity in protein kinase A JF - Proceedings of the National Academy of Sciences VL - 105 IS - 2 SP - 506 EP - 511 N2 - Allosteric signaling in proteins requires long-range communication mediated by highly conserved residues, often triggered by ligand binding. In this article, we map the allosteric network in the catalytic subunit of protein kinase A using NMR spectroscopy. We show that positive allosteric cooperativity is generated by nucleotide and substrate binding during the transitions through the major conformational states: apo, intermediate, and closed. The allosteric network is disrupted by a single site mutation (Y204A), which also decouples the cooperativity of ligand binding. Because protein kinase A is the prototype for the entire kinome, these findings may serve as a paradigm for describing long-range coupling in other protein kinases. 10.1073/pnas.0709214104 KW - allostery KW - experiment KW - nmr AU - Masterson, Larry AU - Mascioni, Alessandro AU - Traaseth, Nathaniel AU - Taylor, Susan AU - Veglia, Gianluigi PY - 2008/01/15/ UR - http://dx.doi.org/10.1073/pnas.0709214104 ER -

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