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Although STIM1 dimers are known to bind directly to the cytosolic C termini of the six Orai1 subunits (SUs) that form the channel hexamer, the dependence of channel activation and selectivity on the number of occupied binding sites is not well understood.
Thus the presence of these binding sites is not sufficient to efficiently target SHM/GCV at the robust levels observed in wild-type DT40 cells.
In this alignment the central β-sheets are closer in space, even though an alignment that simultaneously superimposes both the central sheets and the binding sites is not possible due to the above-mentioned permutation.
The role of these binding sites is not completely established.
The assignment of target genes for binding sites is not trivial.
It has been shown that convergent evolution of enzyme binding sites is not a rare phenomenon (Gherardini et al., 2007).
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Binding of Cry1Ac in the resistant insects remains unaltered, confirming that Cry1Ac binding sites are not shared with those of Cry2Ab.
Flanking sequences – 20-nt-long PCR primer binding sites are not shown in the figure.
Although most individual Ubx binding sites are not evolutionarily conserved, the overall enhancer architecture clusters of low affinity binding sites is maintained and required for enhancer function.
The derivatives with bulky substituents on the myo-inositol moiety significantly activated PKCα, but their binding sites were not the same as that of phorbol ester.
While transcription factor binding sites are not completely conserved, we demonstrate that these sequences are bona fide regulatory elements, despite variable regulatory architecture.
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