4joi

From Proteopedia

(Difference between revisions)

Revision as of 15:22, 25 December 2014

Crystal structure of the human telomeric Stn1-Ten1 complex

Structural highlights

4joi is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4jqf
Gene:	OBFC1, STN1 (Homo sapiens), TEN1, C17orf106 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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] [TEN1L_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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4joi"

@@ Line 7: / Line 7: @@
 <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=4joi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4joi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4joi RCSB], [http://www.ebi.ac.uk/pdbsum/4joi PDBsum]</span></td></tr>
 </table>
+== 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>  [[http://www.uniprot.org/uniprot/TEN1L_HUMAN TEN1L_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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4joi

From Proteopedia

Revision as of 15:22, 25 December 2014

Crystal structure of the human telomeric Stn1-Ten1 complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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