1va3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,827 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,827 edits
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1va3.png|left|200px]]


{{STRUCTURE_1va3| PDB=1va3 |  SCENE= }}
==Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 3)==
<StructureSection load='1va3' size='340' side='right'caption='[[1va3]]' scene=''>
== Structural highlights ==
<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>
</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=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>
</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>
<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.


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


{{ABSTRACT_PUBMED_15609997}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1va3" style="background-color:#fffaf0;"></div>
[[1va3]] is a 1 chain structure with 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=1VA3 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:015609997</ref><references group="xtra"/>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Kobayashi, Y.]]
[[Category: Large Structures]]
[[Category: Ohkubo, T.]]
[[Category: Kobayashi Y]]
[[Category: Oka, S.]]
[[Category: Ohkubo T]]
[[Category: Shiraishi, Y.]]
[[Category: Oka S]]
[[Category: Sugiura, Y.]]
[[Category: Shiraishi Y]]
[[Category: Yoshida, T.]]
[[Category: Sugiura Y]]
[[Category: C2h2 type zinc finger]]
[[Category: Yoshida T]]
[[Category: Dna-binding protein]]
[[Category: Transcription]]
[[Category: Transcription factor]]
Retrieved from "https://proteopedia.org/1va3"