Objective In order to obtain mouse LHCGR extracellular domain protein(LHCGR-1),the structure and physicochemical properties of LHCGR-1 protein were analyzed,which laid a foundation for the study of the function of this protein and the screening of small molecule compounds interacting with it.Method The target gene Lhcgr-1 was synthesized according to the amino acid sequence of mouse LHCGR in NCBI.After bioinformatics analysis,the gene was inserted into the expression vector pET-28a(+)and trans-formed into BL21(DE3)receptor cells.The recombinant protein pET-28a-LHCGR-1 was induced by IPTG and identified by SDS-PAGE and Western Blot.After that,the protein was purified,and the interaction between the protein and LH and CG was predicted by molecular docking technique.Results The molecular weight of the LHCGR-1 protein was estimated to be 40 749.08,composed of 367 amino acids,and the theoretical isoelectric point value was 5.47.There were 29 serine sites,10 threonine sites and 5 tyrosine sites in the amino acid sequence.The recombinant plasmid pET-28a-LHCGR-1 was constructed successfully and the purified target protein was obtained.The molecular docking results showed that the target protein could form stable complexes with LH and CG through vari-ous interactions,so as to play its original biological functions.Conclusion The prokaryotic expression system of mouse extracellular do-main protein LHCGR-1 in Escherichia coli was successfully constructed and the purified protein was obtained.The biological function of the protein was predicted by molecular linkage,suggesting that the protein could be used in subsequent studies.
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