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As OMAB fails to detect assemblies smaller than a trimer, possibly due to steric hindrance as a result of the difference in size, alternative smaller binding structures should be considered to accomplish an oligomer-specific effect targeting e.g. dimeric species.
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Optimally, and especially for protein kinases, a broad range of crystal structures should be obtained to characterize target flexibility, structure modulation via co-factor binding or posttranslational modification, ligand induced conformational changes, and off-target complex structures for selectivity optimization.
In each case, the structures should be interpreted in the context of a kinetic thermodynamic model for ligand binding and catalysis.
Immigration structures should be about finding ways to be compassionate.
Given that BAK1 has no BL-binding activity, their interactions observed in the structure should be dependent on binding of BL to BRI1LRR.
So no conformational adjustment of the RNA structure should be required on binding to L7Ae.
The structure should be named the 9-11 Tower.
Regarding I2, previous studies suggested a major role for the RVxF motif along with secondary binding sites which should be intrinsically structured for efficient binding to PP1c [ 33- 35].
Its binding site should be well characterized.
The structure therefore provides no direct information on ATP binding, and this should be borne in mind as a caveat for interpretation.
Next, the binding of metal should be optimized toward the folded state rather than the unfolded state while keeping the structure flexible enough to allow for metal and substrate binding.
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