Extended Data Fig. 7: CtIP, Sae2, and Ctp1 are all predicted to interact with Rad50 in a similar manner. | Nature Structural & Molecular Biology

Extended Data Fig. 7: CtIP, Sae2, and Ctp1 are all predicted to interact with Rad50 in a similar manner.

From: DNA-PK and the TRF2 iDDR inhibit MRN-initiated resection at leading-end telomeres

Extended Data Fig. 7

(a) Multiple Sequence Alignment (MSA) of CtIP proteins from vertebrate and invertebrate species using NCBI MSA Viewer from an alignment using Multiple Sequence Comparison by Log-Expectation (MUSCLE). Vertical lines are colored by conservation where red indicates highly conserved and blue indicates lower conservation. Alignment positions with gaps are not colored. (b) Representative AlphaFold-Multimer models for CtIP-Rad50, Sae2-Rad50, and Ctp1-Rad50. Important CDK and ATM/Tel1 sites are indicated as well as the residue in the ATM site position on Ctp1. (c) AlphaFold-Multimer Predicted Aligned Error (PAE; top; representative of five ranked models generated with default parameters) plot for S. cerevisiae Sae2-Rad50 and predicted Local Distance Difference Test (pLDDT; bottom) plot across Sae2 from the ranked models. (d) Representative AlphaFold-Multimer models for CtIP-Rad50, Sae2-Rad50, and Ctp1-Rad50. Important CDK and ATM/Tel1 sites are indicated as well as the residue in the ATM site position on Ctp1.

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