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@article{1375133,
author = {Kivi, Rait and Solovjova, Karina and Haljasorg, Tiv and Arukuusk, Piret and Jarv, Jaak},
article_location = {NEW YORK},
article_number = {6},
doi = {http://dx.doi.org/10.1007/s10930-016-9691-9},
keywords = {cAMP-dependent protein kinase catalytic subunit; Allosteric regulation mechanism; ATP binding; Peptide binding; Ligand structure effect},
language = {eng},
issn = {1572-3887},
journal = {The Protein Journal},
title = {Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits},
url = {http://link.springer.com/article/10.1007%2Fs10930-016-9691-9},
volume = {35},
year = {2016}
}
TY - JOUR
ID - 1375133
AU - Kivi, Rait - Solovjova, Karina - Haljasorg, Tiv - Arukuusk, Piret - Jarv, Jaak
PY - 2016
TI - Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits
JF - The Protein Journal
VL - 35
IS - 6
SP - 459-466
EP - 459-466
PB - SPRINGER
SN - 15723887
KW - cAMP-dependent protein kinase catalytic subunit
KW - Allosteric regulation mechanism
KW - ATP binding
KW - Peptide binding
KW - Ligand structure effect
UR - http://link.springer.com/article/10.1007%2Fs10930-016-9691-9
L2 - http://link.springer.com/article/10.1007%2Fs10930-016-9691-9
N2 - The allosteric influence of adenosine triphosphate (ATP) on the binding effectiveness of a series of peptide inhibitors with the catalytic subunit of 3'5'-cyclic adenosine monophosphate dependent protein kinase was investigated, and the dependence of this effect on peptide structure was analyzed. The allosteric effect was calculated as ratio of peptide binding effectiveness with the enzyme-ATP complex and with the free enzyme, quantified by the competitive inhibition of the enzyme in the presence of ATP excess, and by the enzyme-peptide complex denaturation assay, respectively It was found that the principle "better binding-stronger allostery" holds for interactions of the studied peptides with the enzyme, indicating that allostery and peptide binding with the free enzyme are governed by the same specificity pattern. This means that the allosteric regulation does not include new ligand-protein interactions, but changes the intensity (strength) of the interatomic forces that govern the complex formation in the case of each individual ligand. We propose that the allosteric regulation can be explained by the alteration of the intrinsic dynamics of the protein by ligand binding, and that this phenomenon, in turn, modulates the ligand off-rate from its binding site as well as the binding affinity. The positive allostery could therefore be induced by a reduction in the enzyme's overall intrinsic dynamics.
ER -
KIVI, Rait, Karina SOLOVJOVA, Tiv HALJASORG, Piret ARUKUUSK and Jaak JARV. Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits. \textit{The Protein Journal}. NEW YORK: SPRINGER, 2016, vol.~35, No~6, p.~459-466. ISSN~1572-3887. Available from: https://dx.doi.org/10.1007/s10930-016-9691-9.
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