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Increasing Affinity of Interferon-gamma Receptor 1 to Interferon-gamma by Computer-Aided Design

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F13%3A00420825" target="_blank" >RIV/86652036:_____/13:00420825 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1155/2013/752514" target="_blank" >http://dx.doi.org/10.1155/2013/752514</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1155/2013/752514" target="_blank" >10.1155/2013/752514</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Increasing Affinity of Interferon-gamma Receptor 1 to Interferon-gamma by Computer-Aided Design

  • Original language description

    We describe a computer-based protocol to design protein mutations increasing binding affinity between ligand and its receptor. The method was applied to mutate interferon-gamma receptor 1 (IFN-gamma-Rx) to increase its affinity to natural ligand IFN-gamma, protein important for innate immunity. We analyzed all four available crystal structures of the IFN-gamma-Rx/IFN-gamma complex to identify 40 receptor residues forming the interface with IFN-gamma. For these 40 residues, we performed computational mutation analysis by substituting each of the interface receptor residues by the remaining standard amino acids. The corresponding changes of the free energy were calculated by a protocol consisting of FoldX and molecular dynamics calculations. Based on thecomputed changes of the free energy and on sequence conservation criteria obtained by the analysis of 32 receptor sequences from 19 different species, we selected 14 receptor variants predicted to increase the receptor affinity to IFN-ga

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    EI - Biotechnology and bionics

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GAP305%2F10%2F2184" target="_blank" >GAP305/10/2184: Structure-function relationships underlying protein-protein interactions</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2013

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    BIOMED RESEARCH INTERNATIONAL

  • ISSN

    2314-6133

  • e-ISSN

  • Volume of the periodical

  • Issue of the periodical within the volume

    752514

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

  • UT code for WoS article

    000325638500001

  • EID of the result in the Scopus database