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One possibility is that the dimer-dimer interactions are important for p63 DNA binding specificity and therefore p63 requires a full site to bind DNA efficiently.
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Full-length angiocidin bound polyubiquitin while three angiocidin recombinant proteins whose putative polyubiquitin binding sites were mutated either failed to bind polyubiquitin or had significantly diminished binding activity.
Phosphorylation of four threonine sites in the middle domain of Ezh2 by Cdk1 mediates full interaction to bind to Smurf2 for its degradation.
The mutant full-length protein appears to bind DNA normally but is deficient in transcriptional activation.
Results showed that the full-length TB10 is required to bind with E-Tmod, and the TB10 binding site on E-Tmod partially overlaps with the actin binding site on E-Tmod.
In order to determine TLX binding site to pVHL, Cos-1 cells were cotransfected with Flag-TLX and HA-full-length VHL30, or the deletion mutant VHL30Δ95-123, which failed to bind microtubules (Hergovich et al., 2006).
Then, prebound ATP together with Mg ion or newly bound Mg-ADP bridges two halves of the degenerate site to induce its full closure and NBD dimerization.
However, only site 1 is able to bind PP2A1 holoenzyme.
Subsequently, hnRNP-U binds to the same site to further augment OPN promoter activation.
The Fc protein has – except for an antigen-binding site – all properties of a full-size IgG1, i.e. the ability to bind Fcγ-receptors, the complement activator C1q and the neonatal Fc receptor (FcRn).
Similarly, protein factors attempt to bind their target sites.
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