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Figure 6
Structural interface between the FHA and BRCT1 domains of Sp Nbs1 and Sc Xrs2, highlighting structural analogy. (a) Structural overlay of Sp Nbs1 in its Ctp1-bound (PDB entry 3huf, green) and apo (PDB entry 3hue, blue) states (Williams et al., 2009View full citation). Upon Ctp1 binding, residue Arg16 within the FHA domain undergoes a conformational flip, acting as a molecular switch that disrupts its interaction with BRCT1-domain residues Glu193 and Asp194. (b) In Sc Xrs2, FHA-domain residues Arg5 and Ser19 are positioned in proximity to BRCT1-domain residue Asp201, forming an interface structurally analogous to that observed in Sp Nbs1 in (a).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 81| Part 9| September 2025| Pages 365-373
https://doi.org/10.1107/S2053230X25006867
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