English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

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- γ  receptor 1 (IFN- γ -Rx) to increase its affinity to natural ligand IFN- γ , protein important for innate immunity. We analyzed all four available crystal structures of the IFN- γ -Rx/IFN- γ  complex to identify 40 receptor residues forming the interface with IFN- γ . 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 the computed 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- γ . These variants were expressed as recombinant proteins in  Escherichia coli , and their affinities to IFN- γ  were determined experimentally by surface plasmon resonance (SPR). The SPR measurements showed that the simple computational protocol succeeded in finding two receptor variants with affinity to IFN- γ  increased about fivefold compared to the wild-type receptor.

biomed research international

Increasing Affinity of Interferon-<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="M1"><mml:mrow><mml:mi mathvariant="bold">γ</mml:mi></mml:mrow></mml:math>Receptor 1 to Interferon-<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="M2"><mml:mrow><mml:mi mathvariant="bold">γ</mml:mi></mml:mrow></mml:math>by Computer-Aided Design

Increasing Affinity of Interferon-γReceptor 1 to Interferon-γby Computer-Aided Design