A Shared Docking Motif in TRF1 and TRF2 Used for Differential Recruitment of Telomeric Proteins

The binding of and to their shared binding partner and other shelterin accessory factors takes place in two different ways. binds to through its TRF homology (TRFH) domain, which is also used for binding with shelterin-associated factor . The binding site of lies outside the TRFH domain. Instead, the TRFH domain functions as docking site for shelterin accessory factor . Interestingly, and the TRFH domain do not interact.

Shelterin is a six-protein complex, protecting telomeres in mammalian cells. It contains the two closely related proteins and , which recruit various proteins to the telomeres.

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