Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F16%3A00093864" target="_blank" >RIV/00216224:14740/16:00093864 - isvavai.cz</a>

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs10930-016-9691-9" target="_blank" >http://link.springer.com/article/10.1007%2Fs10930-016-9691-9</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10930-016-9691-9" target="_blank" >10.1007/s10930-016-9691-9</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

The Protein Journal

ISSN

1572-3887

e-ISSN

—

Svazek periodika

35

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

459-466

Kód UT WoS článku

000389918500008

EID výsledku v databázi Scopus

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