5HKP

Crystal structure of mouse Tankyrase/human TRF1 complex

Summary for 5HKP

• Entry DOI: 10.2210/pdb5hkp/pdb
• Descriptor: Tankyrase-1, Telomeric repeat-binding factor 1 (3 entities in total)
• Functional Keywords: tankyrase, trf1, telomere, transferase - signaling protein complex, transferase / signaling protein
• Biological source: Mus musculus (Mouse); More
• Cellular location: Cytoplasm : Q6PFX9; Nucleus: P54274
• Total number of polymer chains: 4
• Total formula weight: 88928.55

Authors

Wang, Z.,Li, B.,Rao, Z.,Xu, W. (deposition date: 2016-01-14, release date: 2016-03-23, Last modification date: 2023-09-27)

Primary citation

Li, B.,Qiao, R.,Wang, Z.,Zhou, W.,Li, X.,Xu, W.,Rao, Z.
Crystal structure of a tankyrase 1-telomere repeat factor 1 complex.
Acta Crystallogr F Struct Biol Commun, 72:320-327, 2016

PubMed Abstract: Telomere repeat factor 1 (TRF1) is a subunit of shelterin (also known as the telosome) and plays a critical role in inhibiting telomere elongation by telomerase. Tankyrase 1 (TNKS1) is a poly(ADP-ribose) polymerase that regulates the activity of TRF1 through poly(ADP-ribosyl)ation (PARylation). PARylation of TRF1 by TNKS1 leads to the release of TRF1 from telomeres and allows telomerase to access telomeres. The interaction between TRF1 and TNKS1 is thus important for telomere stability and the mitotic cell cycle. Here, the crystal structure of a complex between the N-terminal acidic domain of TRF1 (residues 1-55) and a fragment of TNKS1 covering the second and third ankyrin-repeat clusters (ARC2-3) is presented at 2.2 Å resolution. The TNKS1-TRF1 complex crystals were optimized using an `oriented rescreening' strategy, in which the initial crystallization condition was used as a guide for a second round of large-scale sparse-matrix screening. This crystallographic and biochemical analysis provides a better understanding of the TRF1-TNKS1 interaction and the three-dimensional structure of the ankyrin-repeat domain of TNKS.

PubMed: 27050267
DOI: 10.1107/S2053230X16004131

Experimental method

X-RAY DIFFRACTION (2.2 Å)