4JQF

Structure of the C-terminal domain of human telomeric Stn1

4JQF の概要

• エントリーDOI: 10.2210/pdb4jqf/pdb
• 関連するPDBエントリー: 4JOI
• 分子名称: CST complex subunit STN1 (2 entities in total)
• 機能のキーワード: wing-helix-turn-helix (whth) motif, protein binding, pol alpha, ctc1, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q9H668
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20473.26

構造登録者

Bryan, C.F.,Rice, C.T.,Harkisheimer, M.,Schultz, D.,Skordalakes, E. (登録日: 2013-03-20, 公開日: 2013-06-05, 最終更新日: 2024-10-09)

主引用文献

Bryan, C.,Rice, C.,Harkisheimer, M.,Schultz, D.C.,Skordalakes, E.
Structure of the human telomeric stn1-ten1 capping complex.
Plos One, 8:e66756-e66756, 2013

PubMed Abstract: 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.

PubMed: 23826127
DOI: 10.1371/journal.pone.0066756

実験手法

X-RAY DIFFRACTION (1.6 Å)