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Keyword
- androgen receptor1
- AR1
- chemical shift perturbation1
- CSP1
- differential scanning calorimetry1
- DNA-binding protein1
- DSC1
- electrophoretic mobility shift assay1
- EMSA1
- heteronuclear single quantum coherence1
- HSQC1
- HTD1
- hybrid Tudor domain1
- isothermal titration calorimetry1
- ITC1
- NMR1
- nuclear magnetic resonance1
- nuclear magnetic resonance (NMR)1
- protein motif1
- protein stability1
- protein structure1
- RB1
- RBBP11
- RMSD1
- Tudor domain1
Protein Structure and Folding
2 Results
- Research ArticleOpen Access
Structural basis for the DNA-binding activity of human ARID4B Tudor domain
Journal of Biological ChemistryVol. 296100506Published online: March 3, 2021- Jie Ren
- Hongwei Yao
- Wanhui Hu
- Sarah Perrett
- Weibin Gong
- Yingang Feng
Cited in Scopus: 5Human ARID4A and ARID4B are homologous proteins that are important in controlling gene expression and epigenetic regulation but have distinct functions. Previous studies have shown that the N-terminal domain of ARID4A is an unusual interdigitated double Tudor domain with DNA-binding activity. However, how the Tudor domain of ARID4B differs from that of ARID4A remains unknown. Here, we found that the ARID4B Tudor domain has significantly weaker DNA affinity than the ARID4A Tudor domain despite sharing more than 80% sequence identity. - Protein Structure and Folding, Protein Synthesis and DegradationOpen Access
Evolutionarily Conserved Binding of Translationally Controlled Tumor Protein to Eukaryotic Elongation Factor 1B
Journal of Biological ChemistryVol. 290Issue 14p8694–8710Published online: January 29, 2015- Huiwen Wu
- Weibin Gong
- Xingzhe Yao
- Jinfeng Wang
- Sarah Perrett
- Yingang Feng
Cited in Scopus: 24Translationally controlled tumor protein (TCTP) is an abundant protein that is highly conserved in eukaryotes. However, its primary function is still not clear. Human TCTP interacts with the metazoan-specific eukaryotic elongation factor 1Bδ (eEF1Bδ) and inhibits its guanine nucleotide exchange factor (GEF) activity, but the structural mechanism remains unknown. The interaction between TCTP and eEF1Bδ was investigated by NMR titration, structure determination, paramagnetic relaxation enhancement, site-directed mutagenesis, isothermal titration calorimetry, and HADDOCK docking.