Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation.
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.
Trewhella
Jill
J
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia. jtrewhella@usyd.edu.au
D001665:Binding Sites; D020134:Catalytic Domain; D000242:Cyclic AMP / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry* / Q000378:metabolism; D019281:Dimerization; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry; D008958:Models, Molecular; D009502:Neutrons; D011485:Protein Binding; D011487:Protein Conformation; D012542:Scattering, Radiation; D014961:X-Ray Diffraction
D007527:Isoenzymes; D000242:Cyclic AMP; D017868:Cyclic AMP-Dependent Protein Kinases