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The basis of this selectivity relies on protein-protein interactions between the E3 ubiquitin ligase and the target protein, as illustrated by engaged proteins that are not degraded as a result of unstable ternary complexes with PROTAC-recruited E3 ligases.
The molecular basis of this selectivity remains unknown.
To examine the structural basis of this selectivity, we compared the sequences and structures of these two proteins.
Using molecular modelling and biochemical studies, we explain the basis of this selectivity.
Further analysis of the critical targets of the oncogenic ETS factors is needed to reveal the basis of this selectivity.
Thus, these paradoxical results suggest that a cell-specific mechanism is involved in MSC recruitment induced by HYAL and that the basis of this selectivity requires further investigation.
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The structural basis of this NGR selectivity is still unknown.
The basis of this surprising selectivity may have a number of mechanisms.
An X-ray crystal structure of one of the designed compounds bound to ERRγ LBD confirms the molecular basis of the selectivity.
An X-ray crystal structure of one of the designed compounds bound to ERRgamma LBD confirms the molecular basis of the selectivity.
In humans, the structural basis of the selectivity of genistein for ERβ versus ERα has been linked to two critical positions in the ligand binding pocket, Met 336 and Ile 373, which are replaced by a Leu and a Met respectively in ERα ([23]; see Figure 6A).
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