1sp1

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[[Image:1sp1.png|left|200px]]
 
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==NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F3, MINIMIZED AVERAGE STRUCTURE==
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<StructureSection load='1sp1' size='340' side='right'caption='[[1sp1]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sp1]] 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=1SP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SP1 FirstGlance]. <br>
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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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<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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{{STRUCTURE_1sp1| PDB=1sp1 | SCENE= }}
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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=1sp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp1 OCA], [https://pdbe.org/1sp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sp1 RCSB], [https://www.ebi.ac.uk/pdbsum/1sp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp1 ProSAT]</span></td></tr>
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</table>
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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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== Publication Abstract from PubMed ==
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The carboxyl terminus of transcription factor Sp1 contains three contiguous Cys2-His2 zinc finger domains with the consensus sequence Cys-X2-4-Cys-X12-His-X3-His. We have used standard homonuclear two-dimensional NMR techniques to solve the solution structures of synthetic peptides corresponding to the last two zinc finger domains (Sp1f2 and Sp1f3, respectively) of Sp1. Our studies indicate a classical Cys2-His2 type fold for both the domains differing from each other primarily in the conformation of Cys-X2-Cys (beta-type I turn) and Cys-X4-Cys (beta-type II turn) elements. There are, however, no significant differences in the metal binding properties between the Cys-X4-Cys (Sp1f2) and Cys-X2-Cys (Sp1f3) subclasses of zinc fingers. The free solution structures of Sp1f2 and Sp1f3 are very similar to those of the analogous fingers of Zif268 bound to DNA. There is NMR spectral evidence suggesting that the Arg-Asp buttressing interaction observed in the Zif-268.DNA complex is also preserved in unbound Sp1f2 and Sp1f3. Modeling Sp1-DNA complex by overlaying the Sp1f2 and Sp1f3 structures on Zif268 fingers 1 and 2, respectively, predicts the role of key amino acid residues, the interference/protection data, and supports the model of Sp1-DNA interaction proposed earlier.
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===NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F3, MINIMIZED AVERAGE STRUCTURE===
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Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition.,Narayan VA, Kriwacki RW, Caradonna JP J Biol Chem. 1997 Mar 21;272(12):7801-9. PMID:9065444<ref>PMID:9065444</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1sp1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 9065444 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9065444}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1SP1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP1 OCA].
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==Reference==
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Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition., Narayan VA, Kriwacki RW, Caradonna JP, J Biol Chem. 1997 Mar 21;272(12):7801-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9065444 9065444]
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[[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: Caradonna, J P.]]
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[[Category: Caradonna JP]]
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[[Category: Kriwacki, R W.]]
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[[Category: Kriwacki RW]]
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[[Category: Narayan, V A.]]
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[[Category: Narayan VA]]
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[[Category: Sp1]]
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[[Category: Transcription activation]]
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[[Category: Zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:18:38 2008''
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Current revision

NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F3, MINIMIZED AVERAGE STRUCTURE

PDB ID 1sp1

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