Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation.

European Biophysics Journal : EBJ
J Trewhella

Abstract

Using small-angle solution scattering and neutron contrast variation, we have studied the structure of the multi-subunit protein kinase A. We have gained insights into how nature can take a set of common structural domains (or themes) and modulate their interactions via sequence variations and second messenger mediated signaling to affect enzyme activity and receptor binding important for targeting this multi-function enzyme to specific sub-cellular locations. These studies demonstrate the power of neutron contrast variation to expand our knowledge of the dynamic supra-molecular structures that carry out biological function.

References

Nov 5, 1997·Current Opinion in Structural Biology·J Trewhella
Mar 13, 1999·Nature Structural Biology·M G NewlonP A Jennings
Oct 14, 2000·Annual Review of Physical Chemistry·M E WallJ Trewhella
Dec 6, 2001·Journal of Molecular Evolution·Jaume M Canaves, Susan S Taylor
Jan 19, 2002·The Journal of Biological Chemistry·Chang-Shung TungJill Trewhella
Feb 9, 2002·The Journal of Biological Chemistry·Reidun KopperudStein Ove Døskeland
Jul 18, 2002·Annals of the New York Academy of Sciences·Paul S Amieux, G Stanley McKnight
Jan 13, 2004·Physiological Reviews·Kjetil Taskén, Einar Martin Aandahl
Feb 27, 2004·The Journal of Biological Chemistry·William T HellerJill Trewhella
May 12, 2004·Biochemistry·Dominico VigilJill Trewhella

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Citations

Jul 14, 2009·Journal of Molecular Biology·Jianquan LiZimei Bu
Jun 7, 2011·International Journal of Mass Spectrometry·Jun H LeeDarren E Casteel

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