btb poz domain

Zinc Finger And BTB Domaincontaining Protein 16 BTBPOZ Domain PNG

BTBPOZ domaincontaining protein 7 Positive Control A56459

Details of the BTBPOZ domain dimer A BTBPOZ conserved residues

The BTBPOZ domain family and its relationship to PLZFBTBPOZ A

The BTBPOZ domain family and its relationship to PLZFBTBPOZ A

The BTBPOZ domain family and its relationship to PLZFBTBPOZ A

Transcriptional repression by fulllength PLZF with BTBPOZ mutations

Sequence alignment of the BTBPOZ domains Among the 40 BTBPOZ domains

Figure 5 from Structurefunction studies of the BTBPOZ transcriptional

Table 1 from Structurefunction studies of the BTBPOZ transcriptional

Figure 4 from Structurefunction studies of the BTBPOZ transcriptional

Figure 1 from The BTBPOZ domain of the regulatory proteins Bric brac

Figure 2 from The BTBPOZ domain of the regulatory proteins Bric brac

The BTBPOZ domain is necessary for cKrox function during lineage

The BTBPOZ domain containing the NCoR interaction region is required

Y2H analysis of GAF direct BTBPOZ domain partners A The structure

Equilibrium sedimentation of the recombinant BTB POZ domain of PLZF

SOLUTION Backbone resonance assignment of the bcl6 btb poz domain

The BTBPOZ Domain of NPR1 Is Required for PR1 Induction Download

The BTBPOZ Domain of NPR1 Is Required for PR1 Induction Download

The BTBPOZ Domain of NPR1 Is Required for PR1 Induction Download

The BTBPOZ Domain of NPR1 Interacts with the N terminus of TGA2 and

Mitochondrial damage control process by BTBproteins BTBdomain

NPR1 Binds SA to Relieve Sequestration of the Transactivating Domain by

Proposed Role of Kelch Proteins as an E3 Ligase Substrate Adaptor The

The BTBPOZ Domain of NPR1 Interacts with the N terminus of TGA2 and

Human group A SRCR members BTBPOZ D melanogaster kelch protein

Figure 1 from Corepressor SMRT binds the BTB y POZ repressing domain of

Figure 1 from Characterization of Two Novel Nuclear BTBPOZ Domain Zinc

Figure 1 from The Keap1 BTBPOZ Dimerization Function Is Required to

Figure 1 from The Keap1 BTBPOZ Dimerization Function Is Required to

Figure 4 from The integrity of the charged pocket in the BTBPOZ domain

PDF The integrity of the charged pocket in the BTBPOZ domain is

Table 1 from The integrity of the charged pocket in the BTBPOZ domain

PDF The integrity of the charged pocket in the BTBPOZ domain is

BTB/POZ domain GudangMovies21 Rebahinxxi LK21

The BTB/POZ domain (BTB for BR-C, ttk and bab or POZ for Pox virus and Zinc finger) is a structural domain found in proteins across the domain Eukarya. Given its prevalence in eukaryotes and its absence in Archaea and bacteria, it likely arose after the origin of eukaryotes. While primarily a protein-protein interaction domain, some BTB domains have additional functionality in transcriptional regulation, cytoskeletal mobility, protein ubiquitination and degradation, and ion channel formation and operation. BTB domains have traditionally been classified by the other structural features present in the protein.




Discovery


The BTB/POZ domain was first described by two independent research groups in 1994. Researchers at UCLA found a conserved 115 amino acid motif in nine Drosophila proteins, including Broad complex, tramtrack, and bric-a-brac, and labelled the conserved region the BTB domain. At the same time, a group at Imperial Cancer Research Fund Laboratories in London discovered the same 120 amino acid motif in a set of otherwise unrelated zinc finger proteins and a set of pox-virus proteins, and thus named the region the POZ domain.




Structure


The motif is approximately 120 amino acids long, with a core fold of 95 amino acids that form five alpha helices and three beta sheets. The alpha helices form two hairpin structures, A1/A2 and A4/A5, out of the first and second and the fourth and fifth alpha helices respectively. The remaining alpha helix, A3, bridges the two. The three beta sheets cap the A1/A2 hairpin. Additional secondary structures can surround this core fold. For example, BTB domains in Kelch proteins, C2H2 zinc finger proteins, and HTH-containing proteins frequently include an additional alpha helix and beta sheet at the N-terminus of the domain.




Function


The BTB domain is primarily a protein-protein interaction domain. In zinc-finger proteins, it commonly forms homodimers with other BTB domains, mediates heteromeric dimerization, and recruits transcriptional corepressors.




References

Kata Kunci Pencarian: btb poz domain

• BTB/POZ domain
• BTB
• Potassium channel tetramerisation domain
• BTBD2
• BACH2
• ABTB1
• BTBD1
• ZBTB32
• SPOP
• Zinc finger and BTB domain-containing protein 16