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| | ==Crystal structure of the BTB domain from FAZF/ZBTB32== | | ==Crystal structure of the BTB domain from FAZF/ZBTB32== |
| - | <StructureSection load='3m5b' size='340' side='right' caption='[[3m5b]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3m5b' size='340' side='right'caption='[[3m5b]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3m5b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M5B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3m5b]] is a 2 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=3M5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M5B FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m52|3m52]], [[3m4t|3m4t]]</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FAZF, TZFP, ZBTB32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3m5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5b OCA], [https://pdbe.org/3m5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m5b RCSB], [https://www.ebi.ac.uk/pdbsum/3m5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5b ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m5b RCSB], [http://www.ebi.ac.uk/pdbsum/3m5b PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ZBT32_HUMAN ZBT32_HUMAN]] 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).<ref>PMID:10572087</ref> | + | [https://www.uniprot.org/uniprot/ZBT32_HUMAN ZBT32_HUMAN] 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).<ref>PMID:10572087</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/3m5b_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/3m5b_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| - | </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/chain_selection.php?pdb_ID=2ata 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=3m5b ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3m5b" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Pomroy, N C]] | + | [[Category: Large Structures]] |
| - | [[Category: Prive, G G]] | + | [[Category: Pomroy NC]] |
| - | [[Category: Stogios, P J]] | + | [[Category: Prive GG]] |
| - | [[Category: Alpha/beta protein]] | + | [[Category: Stogios PJ]] |
| - | [[Category: Btb domain]]
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| - | [[Category: Btb/poz domain]]
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| - | [[Category: Dna binding protein]]
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| - | [[Category: Dna-binding]]
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| - | [[Category: Fancc-interacting protein]]
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| - | [[Category: Fanconi anemia zinc finger protein]]
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| - | [[Category: Faxf]]
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| - | [[Category: Fazf]]
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| - | [[Category: Metal-binding]]
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| - | [[Category: Nucleus]]
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| - | [[Category: Poz domain]]
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| - | [[Category: Protein-protein interaction domain]]
| + | |
| - | [[Category: Repressor]]
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| - | [[Category: Rog]]
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| - | [[Category: Testis zinc finger protein]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Transcription regulator]]
| + | |
| - | [[Category: Tzfp]]
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| - | [[Category: Zbtb32]]
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| - | [[Category: Zinc finger and btb domain-containing protein 32]]
| + | |
| - | [[Category: Zinc-finger]]
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| - | [[Category: Zinc-finger protein]]
| + | |
| - | [[Category: Znf538]]
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| Structural highlights
Function
ZBT32_HUMAN 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).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The BTB domain is a widely distributed protein-protein interaction motif that is often found at the N-terminus of zinc finger transcription factors. Previous crystal structures of BTB domains have revealed tightly interwound homodimers, with the N-terminus from one chain forming a two-stranded anti-parallel beta-sheet with a strand from the other chain. We have solved the crystal structures of the BTB domains from Fanconi anemia zinc finger (FAZF) and Miz1 (Myc-interacting zinc finger 1) to resolutions of 2.0 A and 2.6 A, respectively. Unlike previous examples of BTB domain structures, the FAZF BTB domain is a nonswapped dimer, with each N-terminal beta-strand associated with its own chain. As a result, the dimerization interface in the FAZF BTB domain is about half as large as in the domain-swapped dimers. The Miz1 BTB domain resembles a typical swapped BTB dimer, although it has a shorter N-terminus that is not able to form the interchain sheet. Using cysteine cross-linking, we confirmed that the promyelocytic leukemia zinc finger (PLZF) BTB dimer is strand exchanged in solution, while the FAZF BTB dimer is not. A phylogenic tree of the BTB fold based on both sequence and structural features shows that the common ancestor of the BTB domain in BTB-ZF (bric a brac, tramtrack, broad-complex zinc finger) proteins was a domain-swapped dimer. The differences in the N-termini seen in the FAZF and Miz1 BTB domains appear to be more recent developments in the structural evolution of the domain.
Insights into strand exchange in BTB domain dimers from the crystal structures of FAZF and Miz1.,Stogios PJ, Cuesta-Seijo JA, Chen L, Pomroy NC, Prive GG J Mol Biol. 2010 Jul 30;400(5):983-97. Epub 2010 May 21. PMID:20493880[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hoatlin ME, Zhi Y, Ball H, Silvey K, Melnick A, Stone S, Arai S, Hawe N, Owen G, Zelent A, Licht JD. A novel BTB/POZ transcriptional repressor protein interacts with the Fanconi anemia group C protein and PLZF. Blood. 1999 Dec 1;94(11):3737-47. PMID:10572087
- ↑ Stogios PJ, Cuesta-Seijo JA, Chen L, Pomroy NC, Prive GG. Insights into strand exchange in BTB domain dimers from the crystal structures of FAZF and Miz1. J Mol Biol. 2010 Jul 30;400(5):983-97. Epub 2010 May 21. PMID:20493880 doi:10.1016/j.jmb.2010.05.028
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