4RQI

Structure of TRF2/RAP1 secondary interaction binding site

4RQI の概要

• エントリーDOI: 10.2210/pdb4rqi/pdb
• 分子名称: Telomeric repeat-binding factor 2, Telomeric repeat-binding factor 2-interacting protein 1, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: telomeres, cell cycle
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 103188.00

構造登録者

Miron, S.,Guimaraes, B.,Gaullier, G.,Giraud-Panis, M.-J.,Gilson, E.,Le Du, M.-H. (登録日: 2014-11-03, 公開日: 2016-02-10, 最終更新日: 2024-02-28)

主引用文献

Gaullier, G.,Miron, S.,Pisano, S.,Buisson, R.,Le Bihan, Y.V.,Tellier-Lebegue, C.,Messaoud, W.,Roblin, P.,Guimaraes, B.G.,Thai, R.,Giraud-Panis, M.J.,Gilson, E.,Le Du, M.H.
A higher-order entity formed by the flexible assembly of RAP1 with TRF2.
Nucleic Acids Res., 44:1962-1976, 2016

PubMed Abstract: Telomere integrity is essential to maintain genome stability, and telomeric dysfunctions are associated with cancer and aging pathologies. In human, the shelterin complex binds TTAGGG DNA repeats and provides capping to chromosome ends. Within shelterin, RAP1 is recruited through its interaction with TRF2, and TRF2 is required for telomere protection through a network of nucleic acid and protein interactions. RAP1 is one of the most conserved shelterin proteins although one unresolved question is how its interaction may influence TRF2 properties and regulate its capacity to bind multiple proteins. Through a combination of biochemical, biophysical and structural approaches, we unveiled a unique mode of assembly between RAP1 and TRF2. The complete interaction scheme between the full-length proteins involves a complex biphasic interaction of RAP1 that directly affects the binding properties of the assembly. These results reveal how a non-DNA binding protein can influence the properties of a DNA-binding partner by mutual conformational adjustments.

PubMed: 26748096
DOI: 10.1093/nar/gkv1531

実験手法

X-RAY DIFFRACTION (2.4405 Å)