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4jqf

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jqf RCSB], [http://www.ebi.ac.uk/pdbsum/4jqf PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jqf RCSB], [http://www.ebi.ac.uk/pdbsum/4jqf PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://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>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 08:45, 25 December 2014

Structure of the C-terminal domain of human telomeric Stn1

4jqf, resolution 1.60Å

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