1va2
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1va2.png|left|200px]] | ||
- | < | + | ==Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 2)== |
- | + | <StructureSection load='1va2' size='340' side='right'caption='[[1va2]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1va2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VA2 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1va2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va2 OCA], [https://pdbe.org/1va2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1va2 RCSB], [https://www.ebi.ac.uk/pdbsum/1va2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1va2 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/SP1_HUMAN SP1_HUMAN] Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression.<ref>PMID:10391891</ref> <ref>PMID:11371615</ref> <ref>PMID:11904305</ref> <ref>PMID:14593115</ref> <ref>PMID:16377629</ref> <ref>PMID:17049555</ref> <ref>PMID:16478997</ref> <ref>PMID:16943418</ref> <ref>PMID:18171990</ref> <ref>PMID:18513490</ref> <ref>PMID:18239466</ref> <ref>PMID:18619531</ref> <ref>PMID:18199680</ref> <ref>PMID:19193796</ref> <ref>PMID:20091743</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/1va2_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </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/main_output.php?pdb_ID=1va2 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | To understand the DNA recognition mechanism of zinc finger motifs of transcription factor Sp1, we have determined the solution structure of DNA-binding domain of the Sp1 by solution NMR techniques. The DNA-binding domain of Sp1 consists of three Cys(2)His(2)-type zinc finger motifs. They have typical betabetaalpha zinc finger folds and relatively random orientations. From DNA-binding analysis performed by NMR and comparison between structures determined here and previously reported structures of other zinc fingers, it was assumed that DNA recognition modes of fingers 2 and 3 would be similar to those of fingers of Zif268, in which each finger recognizes four base pairs strictly by using residues at positions -1, 2, 3, and 6 of the recognition helix. On the contrary, finger 1 can use only two residues for DNA recognition, Lys550 and His553 at positions -1 and 3 of the helix, and has more relaxed sequence and site specificity than other Cys(2)His(2) zinc fingers. It is proposed that this relaxed property of finger 1 allows transcription factor Sp1 to bind various DNA sequences with high affinity. | ||
- | + | NMR structure of transcription factor Sp1 DNA binding domain.,Oka S, Shiraishi Y, Yoshida T, Ohkubo T, Sugiura Y, Kobayashi Y Biochemistry. 2004 Dec 28;43(51):16027-35. PMID:15609997<ref>PMID:15609997</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1va2" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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- | == | + | |
- | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Kobayashi | + | [[Category: Large Structures]] |
- | [[Category: Ohkubo | + | [[Category: Kobayashi Y]] |
- | [[Category: Oka | + | [[Category: Ohkubo T]] |
- | [[Category: Shiraishi | + | [[Category: Oka S]] |
- | [[Category: Sugiura | + | [[Category: Shiraishi Y]] |
- | [[Category: Yoshida | + | [[Category: Sugiura Y]] |
- | + | [[Category: Yoshida T]] | |
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Current revision
Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 2)
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Categories: Homo sapiens | Large Structures | Kobayashi Y | Ohkubo T | Oka S | Shiraishi Y | Sugiura Y | Yoshida T