4e6s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:49, 20 March 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e6s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E6S FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e6s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E6S FirstGlance]. <br>
-
</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=4e6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e6s OCA], [https://pdbe.org/4e6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e6s RCSB], [https://www.ebi.ac.uk/pdbsum/4e6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e6s ProSAT]</span></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]] 1.85&#8491;</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=4e6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e6s OCA], [https://pdbe.org/4e6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e6s RCSB], [https://www.ebi.ac.uk/pdbsum/4e6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e6s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/ZSC10_MOUSE ZSC10_MOUSE]] Embryonic stem (ES) cell-specific transcription factor required to maintain ES cell pluripotency. Can both activate and /or repress expression of target genes, depending on the context. Specifically binds the 5'-[GA]CGCNNGCG[CT]-3' DNA consensus sequence. Regulates expression of POU5F1/OCT4, ZSCAN4 and ALYREF/THOC4.<ref>PMID:16971461</ref> <ref>PMID:17628018</ref> <ref>PMID:19740739</ref>
+
[https://www.uniprot.org/uniprot/ZSC10_MOUSE ZSC10_MOUSE] Embryonic stem (ES) cell-specific transcription factor required to maintain ES cell pluripotency. Can both activate and /or repress expression of target genes, depending on the context. Specifically binds the 5'-[GA]CGCNNGCG[CT]-3' DNA consensus sequence. Regulates expression of POU5F1/OCT4, ZSCAN4 and ALYREF/THOC4.<ref>PMID:16971461</ref> <ref>PMID:17628018</ref> <ref>PMID:19740739</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Zfp206 (also named Zscan10) is a transcription factor that plays an important role in maintaining the pluripotent state of embryonic stem cells. Zfp206 is a member of the SCAN-domain family of C(2)H(2) zinc-finger transcription factors. The SCAN domain is a highly conserved motif of 84 residues which mediates the self-association of and heterodimerization between SCAN-domain family transcription factors. The SCAN domain may therefore be the key to the selective oligomerization of and may combinatorially enhance the regulatory versatility of C(2)H(2) zinc fingers. This paper describes crystallization attempts with the SCAN domain of Zfp206 (Zfp206SCAN) and optimization strategies to obtain diffraction-quality crystals. The best diffracting crystal was grown in a solution consisting of 0.3 M ammonium sulfate, 0.1 M Tris-HCl pH 8.6, 25% PEG 3350, 0.1 M ethylenediaminetetraacetic acid disodium salt dehydrate (EDTA) using the hanging-drop vapour-diffusion technique. Optimized crystals diffracted to 1.85 A resolution and belonged to space group I422, with unit-cell parameters a = 67.57, c = 87.54 A. A Matthews analysis indicated the presence of one Zfp206SCAN molecule per asymmetric unit.
+
-
 
+
-
Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206.,Liang Y, Choo SH, Rossbach M, Baburajendran N, Palasingam P, Kolatkar PR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):443-7. Epub, 2012 Mar 27. PMID:22505416<ref>PMID:22505416</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4e6s" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of the SCAN domain from mouse Zfp206

PDB ID 4e6s

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools