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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4joi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JOI FirstGlance]. <br>
<table><tr><td colspan='2'>[[4joi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JOI 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=4joi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4joi OCA], [https://pdbe.org/4joi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4joi RCSB], [https://www.ebi.ac.uk/pdbsum/4joi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4joi 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]] 2.05&#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=4joi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4joi OCA], [https://pdbe.org/4joi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4joi RCSB], [https://www.ebi.ac.uk/pdbsum/4joi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4joi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/STN1_HUMAN STN1_HUMAN] Component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. In addition to telomere protection, the CST complex has probably a more general role in DNA metabolism at non-telomeric sites.<ref>PMID:19854130</ref> <ref>PMID:19648609</ref>  
[https://www.uniprot.org/uniprot/STN1_HUMAN STN1_HUMAN] Component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. In addition to telomere protection, the CST complex has probably a more general role in DNA metabolism at non-telomeric sites.<ref>PMID:19854130</ref> <ref>PMID:19648609</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The identification of the human homologue of the yeast CST in 2009 posed a new challenge in our understanding of the mechanism of telomere capping in higher eukaryotes. The high-resolution structure of the human Stn1-Ten1 (hStn1-Ten1) complex presented here reveals that hStn1 consists of an OB domain and tandem C-terminal wHTH motifs, while hTen1 consists of a single OB fold. Contacts between the OB domains facilitate formation of a complex that is strikingly similar to the replication protein A (RPA) and yeast Stn1-Ten1 (Ten1) complexes. The hStn1-Ten1 complex exhibits non-specific single-stranded DNA activity that is primarily dependent on hStn1. Cells expressing hStn1 mutants defective for dimerization with hTen1 display elongated telomeres and telomere defects associated with telomere uncapping, suggesting that the telomeric function of hCST is hTen1 dependent. Taken together the data presented here show that the structure of the hStn1-Ten1 subcomplex is conserved across species. Cell based assays indicate that hTen1 is critical for the telomeric function of hCST, both in telomere protection and downregulation of telomerase function.
Structure of the human telomeric stn1-ten1 capping complex.,Bryan C, Rice C, Harkisheimer M, Schultz DC, Skordalakes E PLoS One. 2013 Jun 24;8(6):e66756. doi: 10.1371/journal.pone.0066756. Print 2013. PMID:23826127<ref>PMID:23826127</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4joi" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 12:05, 1 March 2024

Crystal structure of the human telomeric Stn1-Ten1 complex

4joi, resolution 2.05Å

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