Document Type

Journal Article

Language

English

Abstract

CXCR1, a member in G-protein coupled receptor (GPCR) family, binds to chemokine interleukin-8 (IL-8) specifically and transduces signals to mediate immune and inflammatory responses. Despite the importance of CXCR1, high-resolution structure determination is hindered by the challenges in crystallization. It has been shown that properly designed mutants with enhanced thermostability, together with fusion partner proteins, can be useful to form crystals for GPCR proteins. In this study, in silico protein design was carried out by using homology modeling and molecular dynamics simulations. To validate the computational modeling results, the thermostability of several mutants and the wild type were measured experimentally. Both computational results and experimental data suggest that the mutant L126W has a significant improvement in the thermostability. This study demonstrated that in silicodesign can guide protein engineering and potentially facilitate protein crystallography research.

Publication Date

3-2019

Source Publication Title

Scientific Reports

Volume

9

Publisher

Nature Research

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

DOI

10.1038/s41598-019-41838-2

Link to Publisher's Edition

https://doi.org/10.1038/s41598-019-41838-2

ISSN (print)

20452322

Included in

Physics Commons

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