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2 edition of Structure and function of the BTB domain. found in the catalog.

Structure and function of the BTB domain.

Khaja Farid Ahmad

Structure and function of the BTB domain.

by Khaja Farid Ahmad

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  • 4 Currently reading

Published .
Written in English


Edition Notes

Thesis (Ph.D.) -- University of Toronto, 2003.

The Physical Object
Pagination204 leaves.
Number of Pages204
ID Numbers
Open LibraryOL22585399M
ISBN 100612847624

heavy chain is composed of four domains: the variable domain (VH), C H1, C H2, and C H3. The light chain is composed of variable domain (VL) and constant domain (CL). All domains in the IgGare members of the Ig-like domain family and share a common Greek-key beta-sandwich structure with conserved intradomain disulfide bonds.   The role of these proteins in Cul3-based SCF-like complexes pose a puzzle, as we do not expect that downstream ZF domains maintain a fixed orientation relative to the BTB domain due to the structurally disordered central region. Further work will be required to understand the structure and function of BTB-ZF proteins in SCF-like complexes.

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. In Arabidopsis, bric-a-brac, tramtrack and broad (BTB) domain scaffold proteins form a family of 80 proteins that have involvement in various signaling pathways. The five members of the subfamily of BTB AND TAZ DOMAIN proteins (BT1-BT5) have a typical domain structure that is only observed in land p .

is a functional organizational structure whose key characteristic is a pyra-mid-shaped hierarchy, which defines the functions carried out and the key management positions assigned to those functions (see Figure ). The size and complexity of the specific health services organization will dictate the particular structure. The BTB domain is a protein–protein interaction motif found throughout eukaryotes. Here we report the identification of two closely related BTB domain-containing proteins, POZ/BTB CONTAINING-PROTEIN 1 (POB1) and POB2, as negative regulators of defense against pathogens. In yeast two-hybrid assays, POB1 and POB2 dimerize through their BTB domains.


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Structure and function of the BTB domain by Khaja Farid Ahmad Download PDF EPUB FB2

Domain Binding and Function. The BTB domain is a protein-protein interaction module consisting of approximately amino acids found in over different proteins from organisms ranging from yeast to humans. The domain was first identified as a conserved sequence element in the developmentally regulated Drosophila proteins B road-complex, T ramtrack and B ric-abrac.

Structure of Keap1 BTB domain in complex with CDDO. The Keap1 antagonist CDDO-Me is poorly soluble in aqueous solution, and so we chose to study the binding of the corresponding carboxylic acid CDDO which is more soluble (Figure 2A).After soaking with CDDO there was clear evidence for covalent modification of Cyswith electron density supportive of ordered compound Cited by:   The BTB domain (also known as the POZ domain) is an evolutionarily conserved protein–protein interaction motif found at the N terminus of 5–10% of C2H2-type zinc-finger transcription factors, as well as in some actin-associated proteins bearing the kelch motif.

Many BTB proteins are transcriptional regulators that mediate gene expression through the control of chromatin by: BibTeX @MISC{Li_structure-functionstudies, author = {Xinmin Li and Hongzhuang Peng and David C.

Schultz and Jesus M. Lopez-guisa and Frank J. Rauscher Iii and Ronen Marmorstein}, title = {Structure-Function Studies of the BTB/POZ Transcriptional Repression Domain from the Promyelocytic Leukemia Zinc Finger Oncoprotein 1}, year = {}}.

The structure of the BTB domain of the promyelocytic leukemia zinc finger (PLZF) protein has been determined by X-ray crystallography and reveals a tightly intertwined dimer with an extensive hydrophobic interface [(PUBMED)]. A surface-exposed groove lined with conserved amino acids is formed at the dimer interface, suggesting a peptide.

The role of these proteins in Cul3-based SCF-like complexes pose a puzzle, as we do not expect that downstream ZF domains maintain a fixed orientation relative to the BTB domain due to the structurally disordered central region.

Further work will be required to understand the structure and function of BTB-ZF proteins in SCF-like complexes. The BTB domain is a highly conserved protein-protein interaction motif present in over human BTB proteins, 43 of which are BTB-ZF proteins with a similar architecture as the BCL6 protein (Stogios et al., ).

In all cases known to date, BTB domain dimerization, and possibly BTB-mediated oligomerization, is required for the normal. BTB (broad-complex, tramtrack and bric à brac) domain-containing proteins are involved in a wide variety of biological processes, such as transcription regulation 1, 2, cytoskeletal arrangement 3, 4, ion conductance and protein ubiquitination 6, 7, 8, domain is typically found as a single copy at the N terminus of proteins that have one other identified domain at the C terminus.

mined the Å crystal structure of the BTB/POZ domain from PLZF (PLZF-BTB/POZ), and have carried out biochemical analysis of PLZF-BTB/POZ harboring site-directed mutations to probe structure-function relationships. The structure reveals a novel a/b homodimeric fold in which dimer interactions occur along two surfaces of the protein subunits.

Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein. Li X(1), Peng H, Schultz DC, Lopez-Guisa JM, Rauscher FJ 3rd, Marmorstein R. Author information: (1)The Wistar Institute, University of Pennsylvania, PhiladelphiaUSA.

DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor. Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells (By similarity).

Bach1 was shown to impair ischemia-induced determine whether the anti-angiogenic effect of Bach1 during recovery from peripheral ischemic injury is mediated by the BTB domain, hind-limb ischemia (HLI) was surgically induced in C57BL/6 J mice, and the injured limbs were treated with saline (the NS group) or with adenoviruses coding for GFP (the AdGFP group), for Bach1.

The BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination.

Several BTB domain structures have been experimentally determined, revealing a highly conserved core structure. The BTB domain facilitates protein-protein interactions between KCTD proteins to allow self-assembly or with non-BTB-domain-containing proteins to promote oligomerization.

The X-ray crystal structure of KCTD5 also revealed assemblies of five subunits while tetramers were anticipated [ 16 ]. Several recent investigations have demonstrated that members of the KCTD (Potassium Channel Tetramerization Domain) protein family are involved in fundamental processes. However, the paucity of structural data available on these proteins has frequently prevented the definition of their biochemical role(s).

Fortunately, this scenario is rapidly changing as, in very recent years, several. The function of the BTB domain is therefore likely to be a general one that is not specific to DNA binding proteins or to other transcription factors.

It is currently believed that the BTB domain facilitates homodimer (9–11) or heterodimer formation (3,7,12–22) as well as oligomerization (23,24). We demonstrate that the coactivator function of NPR1 requires the presence of the BTB/POZ core and the oxidation of Cys and Cys, located in the transactivation domain of NPR1.

Finally, using an in vivo labeling technique capable of distinguishing between the reduced and oxidized states of Cys residues, we determined that Cys and Cys.

Based on crystal structure data of the BTB domain from PLZF, we determined such a function arises from BTB domain by deletion mapping of the full gene.

Compared to the other parts of PLZF, the BTB domain exhibits the specific function of angiogenesis inhibition. The structure shown consists of a single BCL6 BTB domain/SMRT BBD peptide complex.

The domain consists of a central cluster of α-helices flanked by short β-sheets at both ends of the molecule.

The dimer contact is mediated by β1, α1, α2, β5 and α6 structures. The BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation.

The BTB domain (Broad-Complex, Tramtrack, and Bric à brac) (1, 2), also known as POZ (poxvirus and zinc finger) (), is an evolutionarily conserved protein–protein interaction domain often found in developmentally regulated transcription domain is strongly implicated in the regulation of gene expression through the local control of chromatin conformation ().Search the world's most comprehensive index of full-text books.

My library.The BTBD9 gene encodes a protein with three structurally conserved domains (Figure (B)). One domain is a bric-à-brac, tramtrack, broad complex (BTB)/pox virus and zinc finger (POZ) domain near the N-terminus, which has been associated in other proteins with a variety of functions including transcriptional regulation (Ahmad et al., ; David et al., ; Melnick et al.,