7y3i
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7y3i]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y3I FirstGlance]. <br> | <table><tr><td colspan='2'>[[7y3i]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y3I FirstGlance]. <br> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</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=7y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y3i OCA], [https://pdbe.org/7y3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y3i RCSB], [https://www.ebi.ac.uk/pdbsum/7y3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y3i ProSAT]</span></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=7y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y3i OCA], [https://pdbe.org/7y3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y3i RCSB], [https://www.ebi.ac.uk/pdbsum/7y3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y3i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SALL4_HUMAN SALL4_HUMAN] Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells.<ref>PMID:23012367</ref> | [https://www.uniprot.org/uniprot/SALL4_HUMAN SALL4_HUMAN] Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells.<ref>PMID:23012367</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Spalt-like 4 transcription factor (SALL4) plays an essential role in controlling the pluripotent property of embryonic stem cells via binding to AT-rich regions of genomic DNA, but structural details on this binding interaction have not been fully characterized. Here, we present crystal structures of the zinc finger cluster 4 (ZFC4) domain of SALL4 (SALL4(ZFC4)) bound with different dsDNAs containing a conserved AT-rich motif. In the structures, two zinc fingers of SALL4(ZFC4) recognize an AATA tetranucleotide. We also solved the DNA-bound structures of SALL3(ZFC4) and SALL4(ZFC1). These structures illuminate a common preference for the AATA tetranucleotide shared by ZFC4 of SALL1, SALL3, and SALL4. Furthermore, our cell biology experiments demonstrate that the DNA-binding activity is essential for SALL4 function as DNA-binding defective mutants of mouse Sall4 failed to repress aberrant gene expression in Sall4-/- mESCs. Thus, these analyses provide new insights into the mechanisms of action underlying SALL family proteins in controlling cell fate via preferential targeting to AT-rich sites within genomic DNA during cell differentiation. | ||
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| + | Structural studies of SALL family protein zinc finger cluster domains in complex with DNA reveal preferential binding to an AATA tetranucleotide motif.,Ru W, Koga T, Wang X, Guo Q, Gearhart MD, Zhao S, Murphy M, Kawakami H, Corcoran D, Zhang J, Zhu Z, Yao X, Kawakami Y, Xu C J Biol Chem. 2022 Dec;298(12):102607. doi: 10.1016/j.jbc.2022.102607. Epub 2022 , Oct 17. PMID:36257403<ref>PMID:36257403</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7y3i" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of DNA bound SALL4
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