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
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EI - Biotechnology and bionics
OECD FORD branch
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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
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Volume of the periodical
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Issue of the periodical within the volume
752514
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
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UT code for WoS article
000325638500001
EID of the result in the Scopus database
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