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1va3

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[[Image:1va3.gif|left|200px]]
 
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{{Structure
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==Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 3)==
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|PDB= 1va3 |SIZE=350|CAPTION= <scene name='initialview01'>1va3</scene>
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<StructureSection load='1va3' size='340' side='right'caption='[[1va3]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1va3]] 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=1VA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VA3 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= SP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<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>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1va3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va3 OCA], [https://pdbe.org/1va3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1va3 RCSB], [https://www.ebi.ac.uk/pdbsum/1va3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1va3 ProSAT]</span></td></tr>
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</table>
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'''Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 3)'''
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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==Overview==
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== 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.
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.
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==Disease==
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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>
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Known diseases associated with this structure: Hepatic venoocclusive disease with immunodeficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604457 604457]], Mycobacterium tuberculosis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604457 604457]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1VA3 is a [[Single protein]] structure of 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=1VA3 OCA].
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</div>
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<div class="pdbe-citations 1va3" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15609997 15609997]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kobayashi, Y.]]
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[[Category: Kobayashi Y]]
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[[Category: Ohkubo, T.]]
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[[Category: Ohkubo T]]
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[[Category: Oka, S.]]
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[[Category: Oka S]]
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[[Category: Shiraishi, Y.]]
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[[Category: Shiraishi Y]]
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[[Category: Sugiura, Y.]]
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[[Category: Sugiura Y]]
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[[Category: Yoshida, T.]]
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[[Category: Yoshida T]]
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[[Category: ZN]]
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[[Category: c2h2 type zinc finger]]
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[[Category: dna-binding protein]]
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[[Category: transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:47 2008''
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Current revision

Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 3)

PDB ID 1va3

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