Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3'5'-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články
PubMed
27848106
DOI
10.1007/s10930-016-9691-9
PII: 10.1007/s10930-016-9691-9
Knihovny.cz E-zdroje
- Klíčová slova
- ATP binding, Allosteric regulation mechanism, Ligand structure effect, Peptide binding, cAMP-dependent protein kinase catalytic subunit,
- MeSH
- 2-naftylamin analogy a deriváty chemie MeSH
- adenosintrifosfát chemie metabolismus MeSH
- alosterická regulace MeSH
- alosterické místo MeSH
- AMP cyklický chemie metabolismus MeSH
- barvení a značení metody MeSH
- fluorescenční barviva chemie MeSH
- inhibitory proteinkinas chemie metabolismus MeSH
- katalytická doména MeSH
- kinetika MeSH
- lidé MeSH
- ligandy MeSH
- peptidy chemie metabolismus MeSH
- proteinkinasy závislé na cyklickém AMP chemie metabolismus MeSH
- sekvence aminokyselin MeSH
- termodynamika MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- 2-naftylamin MeSH
- acrylodan MeSH Prohlížeč
- adenosintrifosfát MeSH
- AMP cyklický MeSH
- fluorescenční barviva MeSH
- inhibitory proteinkinas MeSH
- ligandy MeSH
- peptidy MeSH
- proteinkinasy závislé na cyklickém AMP MeSH
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.
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