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However, substitutions at the C3 position of the pyridyl ring result in drops of at least 10-fold in potency and indeed are some of the worst compounds identified— 20, 23, 28, and 34, for example—suggesting that substitutions para to the benzylic carbon are not well-accommodated and thus the R-enantiomer may not bind well in the PvdQ binding pocket.
While the pilus surface as a result of globular packing of major pilin monomers might possess some DNA binding capacity, individual monomers may not bind to DNA.
Indeed, inspection of the solution NMR structure of the isolated murine SH3C does not show an obvious binding grove, suggesting that this domain may not bind to, or bind with low affinity, to target proteins [ 176].
Interestingly, the residues 86 95 subject to ubiquitination of S100A10 are the residues responsible for binding with the AnxA2 N-terminal, suggesting that once ubiquitinated, S100A10 may not bind AnxA2 anymore.
However, it may not bind to a subset of cyclobutane dimers, likely including the thymine dimer.
Without NH4+, the NLP7 protein may not bind to the promoter of NRT1.1, resulting in the lost regulation function of NLP7 to NRT1.1.
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Some of these proteins may not naturally bind to small-molecule ligands; however, 36 of these proteins are enzymes, representing a set of cancer-associated proteins for which ligand-bound structures would be greatly beneficial.
To this end, it appears that CAR activation is a multi-step process and most identified CAR activators may not directly bind to the receptor.
If the isoforms are not able to co-assemble, the observations from the spiking reactions that did not assemble to the levels observed with 4R tau alone indicate 3R tau may not simply bind and release the 4R tau before additional 4R tau is being incorporated, but rather 3R may be sequestering either 4R tau or the inducer.
Note that TF X may not directly bind the target gene.
Alternatively, BCL11A may not directly bind in the β-locus rather produce its effect by protein-protein interactions.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com