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

The result's identifiers

  • Result code in 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>

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    The Protein Journal

  • ISSN

    1572-3887

  • e-ISSN

  • Volume of the periodical

    35

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    459-466

  • UT code for WoS article

    000389918500008

  • EID of the result in the Scopus database