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Ligand Strain and Its Conformational Complexity Is a Major Factor in the Binding of Cyclic Dinucleotides to STING Protein

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00541558" target="_blank" >RIV/61388963:_____/21:00541558 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1002/anie.202016805" target="_blank" >https://doi.org/10.1002/anie.202016805</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/anie.202016805" target="_blank" >10.1002/anie.202016805</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Ligand Strain and Its Conformational Complexity Is a Major Factor in the Binding of Cyclic Dinucleotides to STING Protein

  • Original language description

    STING (stimulator of interferon genes) is a key regulator of innate immunity that has recently been recognized as a promising drug target. STING is activated by cyclic dinucleotides (CDNs) which eventually leads to expression of type I interferons and other cytokines. Factors underlying the affinity of various CDN analogues are poorly understood. Herein, we correlate structural biology, isothermal calorimetry (ITC) and computational modeling to elucidate factors contributing to binding of six CDNs—three pairs of natural (ribo) and fluorinated (2′‐fluororibo) 3′,3′‐CDNs. X‐ray structural analyses of six {STING:CDN} complexes did not offer any explanation for the different affinities of the studied ligands. ITC showed entropy/enthalpy compensation up to 25 kcal mol−1 for this set of similar ligands. The higher affinities of fluorinated analogues are explained with help of computational methods by smaller loss of entropy upon binding and by smaller strain (free) energy.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Angewandte Chemie - International Edition

  • ISSN

    1433-7851

  • e-ISSN

    1521-3773

  • Volume of the periodical

    60

  • Issue of the periodical within the volume

    18

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    7

  • Pages from-to

    10172-10178

  • UT code for WoS article

    000631782200001

  • EID of the result in the Scopus database

    2-s2.0-85103176233