Computer aided protein engineering to enhance the thermo-stability of CXCR1- T4 lysozyme complex.

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 mutan

SUBMITTER: Wang Y 

PROVIDER: S-EPMC6441008 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature