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A novel GTP‐binding protein hGBP3 interacts with NIK/HGK
Author(s) -
Luan Zhidong,
Zhang Yan,
Liu Aihua,
Man Yunfang,
Cheng Lu,
Hu Gengxi
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03467-1
Subject(s) - guanylate kinase , chemistry , guanosine , biochemistry , gtp' , immunoprecipitation , c terminus , microbiology and biotechnology , biology , amino acid , enzyme , gene , membrane protein , membrane
A novel human guanylate‐binding protein (GBP) hGBP3 was identified and characterized. Similar as the two human guanylate‐binding proteins hGBP1 and hGBP2, hGBP3 has the first two motifs of the three classical guanylate‐binding motifs, GXXXXGKS (T) and DXXG, but lacks the N (T) KXD motif. Escherichia coli ‐expressed hGBP3 protein specifically binds to guanosine triphosphate (GTP). Using a yeast two‐hybrid system, it was revealed that the N‐terminal region of hGBP3 binds to the C‐terminal regulatory domain of NIK/HGK, a member of the group I GCK (germinal center kinase) family. This interaction was confirmed by in vitro glutathione‐ S ‐transferase (GST) pull‐down and co‐immunoprecipitation assays.