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The SGT1 HSP90 binding interface was confirmed by searching for mutants that showed specific charge compensation effects.
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For a better resolution, a close-up view of the binding interface was developed.
An identical structural homology at the binding interface was predicted (Fig. 4A and Fig.4B).
It is interesting to notice that this double frameshift (if confirmed) may have little influence on the protein (only the beginning of the receptor binding interface is modified).
The RNA binding interface is also extremely diverse for the four Brix proteins.
In (C) and (D) the amino acids forming the HBGA binding interface are in cyan.
The Norrin Fz4CRD binding interface is conserved between the complex structures.
As noted in our previous study, the RPA32C binding interface is devoid of hydrophobic pockets typically found at protein binding interfaces and, rather, is relatively flat.
This supports the hypothesis that the PRD binding interface is disrupted in the truncation mutant.
The predicted binding mode was confirmed by X-ray crystallography.
Through molecular docking studies the binding interaction was confirmed.
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