1buo: Difference between revisions

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<StructureSection load='1buo' size='340' side='right'caption='[[1buo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1buo' size='340' side='right'caption='[[1buo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1buo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BUO FirstGlance]. <br>
<table><tr><td colspan='2'>[[1buo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BUO FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1buo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1buo OCA], [https://pdbe.org/1buo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1buo RCSB], [https://www.ebi.ac.uk/pdbsum/1buo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1buo ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1buo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1buo OCA], [https://pdbe.org/1buo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1buo RCSB], [https://www.ebi.ac.uk/pdbsum/1buo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1buo ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/ZBT16_HUMAN ZBT16_HUMAN]] Defects in ZBTB16 are the cause of skeletal defects genital hypoplasia and mental retardation (SGYMR) [MIM:[https://omim.org/entry/612447 612447]]. A disorder characterized by mental retardation, craniofacial dysmorphism, microcephaly and short stature. Additional features include absence of the thumbs, hypoplasia of the radii and ulnae, additional vertebrae and ribs, retarded bone age and genital hypoplasia.<ref>PMID:18611983</ref>  Note=A chromosomal aberration involving ZBTB16 may be a cause of acute promyelocytic leukemia (APL). Translocation t(11;17)(q32;q21) with RARA.  
[https://www.uniprot.org/uniprot/ZBT16_HUMAN ZBT16_HUMAN] Defects in ZBTB16 are the cause of skeletal defects genital hypoplasia and mental retardation (SGYMR) [MIM:[https://omim.org/entry/612447 612447]. A disorder characterized by mental retardation, craniofacial dysmorphism, microcephaly and short stature. Additional features include absence of the thumbs, hypoplasia of the radii and ulnae, additional vertebrae and ribs, retarded bone age and genital hypoplasia.<ref>PMID:18611983</ref>  Note=A chromosomal aberration involving ZBTB16 may be a cause of acute promyelocytic leukemia (APL). Translocation t(11;17)(q32;q21) with RARA.
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ZBT16_HUMAN ZBT16_HUMAN]] Probable transcription factor. May play a role in myeloid maturation and in the development and/or maintenance of other differentiated tissues. Probable substrate-recognition component of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.<ref>PMID:14528312</ref>
[https://www.uniprot.org/uniprot/ZBT16_HUMAN ZBT16_HUMAN] Probable transcription factor. May play a role in myeloid maturation and in the development and/or maintenance of other differentiated tissues. Probable substrate-recognition component of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.<ref>PMID:14528312</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1buo ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1buo ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 conformation. In the human promyelocytic leukemia zinc finger (PLZF) protein, the BTB domain has transcriptional repression activity, directs the protein to a nuclear punctate pattern, and interacts with components of the histone deacetylase complex. The association of the PLZF BTB domain with the histone deacetylase complex provides a mechanism of linking the transcription factor with enzymatic activities that regulate chromatin conformation. The crystal structure of the BTB domain of PLZF was determined at 1.9 A resolution and reveals a tightly intertwined dimer with an extensive hydrophobic interface. Approximately one-quarter of the monomer surface area is involved in the dimer intermolecular contact. These features are typical of obligate homodimers, and we expect the full-length PLZF protein to exist as a branched transcription factor with two C-terminal DNA-binding regions. A surface-exposed groove lined with conserved amino acids is formed at the dimer interface, suggestive of a peptide-binding site. This groove may represent the site of interaction of the PLZF BTB domain with nuclear corepressors or other nuclear proteins.
Crystal structure of the BTB domain from PLZF.,Ahmad KF, Engel CK, Prive GG Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12123-8. PMID:9770450<ref>PMID:9770450</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1buo" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ahmad, K F]]
[[Category: Ahmad KF]]
[[Category: Engel, C K]]
[[Category: Engel CK]]
[[Category: Prive, G G]]
[[Category: Prive GG]]
[[Category: Gene regulation]]
[[Category: Promyelocytic leukemia]]
[[Category: Protein structure]]
[[Category: Protein-protein interaction domain]]
[[Category: Transcriptional repressor]]
[[Category: Zinc-finger protein]]

Latest revision as of 06:39, 7 February 2024

BTB DOMAIN FROM PLZF

1buo, resolution 1.90Å

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