4RQI
Structure of TRF2/RAP1 secondary interaction binding site
Summary for 4RQI
| Entry DOI | 10.2210/pdb4rqi/pdb |
| Descriptor | Telomeric repeat-binding factor 2, Telomeric repeat-binding factor 2-interacting protein 1, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | telomeres, cell cycle |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 103188.00 |
| Authors | Miron, S.,Guimaraes, B.,Gaullier, G.,Giraud-Panis, M.-J.,Gilson, E.,Le Du, M.-H. (deposition date: 2014-11-03, release date: 2016-02-10, Last modification date: 2024-02-28) |
| Primary citation | 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 Cited by 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: 26748096DOI: 10.1093/nar/gkv1531 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4405 Å) |
Structure validation
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