中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
A novel GTP-binding protein hGBP3 interacts with NIK/HGK

文献类型:期刊论文

作者Luan, ZD; Zhang, Y; Liu, AH; Man, YF; Cheng, L; Hu, GG
刊名FEBS LETTERS
出版日期2002
卷号530期号:1页码:233-238
关键词human guanylate-binding protein 3 Nck-interacting kinase/HPK/GCK-like kinase yeast two-hybrid screening
通讯作者Hu, GG (reprint author), Chinese Acad Sci, Max Planck Guest Lab, Inst Biochem & Cell Biol, 320 Yye Yang Rd, Shanghai 200031, Peoples R China.,
英文摘要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. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
学科主题Biochemistry & Molecular Biology; Biophysics; Cell Biology
类目[WOS]Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
关键词[WOS]GERMINAL CENTER KINASE ; ENCEPHALOMYOCARDITIS VIRUS ; MOLECULAR-CLONING ; GAMMA-SUBUNIT ; DOMAIN ; ACTIVATION ; INDUCTION ; MEMBRANE ; PATHWAY ; CASCADE
收录类别SCI
语种英语
WOS记录号WOS:000178856900043
版本出版稿
源URL[http://202.127.25.143/handle/331003/2556]  
专题上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式
GB/T 7714
Luan, ZD,Zhang, Y,Liu, AH,et al. A novel GTP-binding protein hGBP3 interacts with NIK/HGK[J]. FEBS LETTERS,2002,530(1):233-238.
APA Luan, ZD,Zhang, Y,Liu, AH,Man, YF,Cheng, L,&Hu, GG.(2002).A novel GTP-binding protein hGBP3 interacts with NIK/HGK.FEBS LETTERS,530(1),233-238.
MLA Luan, ZD,et al."A novel GTP-binding protein hGBP3 interacts with NIK/HGK".FEBS LETTERS 530.1(2002):233-238.

入库方式: OAI收割

来源:上海生物化学与细胞生物学研究所

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