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Figure 4.
Fig. 4. The TRF2-Apollo interaction. (A) ITC measurement of the
interactions of TRF1[TRFH] (red) and TRF2[TRFH] (blue) with the
Apollo[TBM] peptide. (B) Overall structure of the dimeric
TRF2[TRFH]-Apollo[TBM] complex. (C) Superposition of Apollo[TBM]
(orange) and TIN2[TBM] (yellow) reveals a shared F/Y-X-L-X-P
motif. (D) Superposition of the TRF2[TRFH]-Apollo[TBM] and the
TRF2[TRFH]-TIN2[TBM] complexes in the vicinity of the Apollo
helix. The TRF2[TRFH] molecules are colored in cyan
(Apollo[TBM]-bound) and gray (TIN2[TBM]-bound), respectively.
(E) Apollo[TBM] binding is TRF2[TRFH]-specific. The surface
representations show that there is no room for Apollo L500 and
Y504 to fit into the peptide binding site of TRF1[TRFH]. (F) In
vitro ITC binding data of wild-type and mutant
TRF2[TRFH]-Apollo[TBM] interactions. (G) Co-IP data show that
Apollo double-mutant L504E/P506 and TRF2 single-mutant F120A
disrupt the in vivo TRF2-Apollo interaction. (H) Localization of
retrovirally expressed HA-tagged wild type and L506E/P508A
double mutant of Apollo in BJ-hTERT cells.
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