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| | ==Structure of the C-terminal domain of human telomeric Stn1== | | ==Structure of the C-terminal domain of human telomeric Stn1== |
| - | <StructureSection load='4jqf' size='340' side='right' caption='[[4jqf]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4jqf' size='340' side='right'caption='[[4jqf]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jqf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JQF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JQF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jqf]] is a 1 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=4JQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JQF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4joi|4joi]]</td></tr> | + | </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=4jqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqf OCA], [https://pdbe.org/4jqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jqf RCSB], [https://www.ebi.ac.uk/pdbsum/4jqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jqf ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OBFC1, STN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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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> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4jqf" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Bryan, C F]] | + | [[Category: Large Structures]] |
| - | [[Category: Harkisheimer, M]] | + | [[Category: Bryan CF]] |
| - | [[Category: Rice, C T]] | + | [[Category: Harkisheimer M]] |
| - | [[Category: Schultz, D]] | + | [[Category: Rice CT]] |
| - | [[Category: Skordalakes, E]] | + | [[Category: Schultz D]] |
| - | [[Category: Ctc1]]
| + | [[Category: Skordalakes E]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Pol alpha]]
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| - | [[Category: Protein binding]]
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| Structural highlights
Function
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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyake Y, Nakamura M, Nabetani A, Shimamura S, Tamura M, Yonehara S, Saito M, Ishikawa F. RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway. Mol Cell. 2009 Oct 23;36(2):193-206. PMID:19854130 doi:S1097-2765(09)00587-5
- ↑ Wan M, Qin J, Songyang Z, Liu D. OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation. J Biol Chem. 2009 Sep 25;284(39):26725-31. Epub 2009 Aug 1. PMID:19648609 doi:M109.021105
- ↑ Bryan C, Rice C, Harkisheimer M, Schultz DC, Skordalakes E. Structure of the human telomeric stn1-ten1 capping complex. PLoS One. 2013 Jun 24;8(6):e66756. doi: 10.1371/journal.pone.0066756. Print 2013. PMID:23826127 doi:10.1371/journal.pone.0066756
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