Smaller, but significant shift changes indicate that binding may alter this interface by affecting the conformation of the helix-turn-helix motif that constitutes a part of it.
We reasoned that small molecule binding may alter Edc3-mediated regulation of these mRNAs because small molecule binding altered the subcellular localization of both Edc3 and other P-body resident proteins, and that the YjeF_N domain is required for efficient mRNA binding (Ling et al. 2008).
Although demonstration of a causal link requires further investigation, we speculate that injury-associated platelet activation and subsequent fibrinogen binding may alter platelet ability to recognize bacterial components, some of which are ligands of αIIbβ3 [35] 35], and affect their ability to alert and recruit cells of the immune system [8].
Our results, when combined with those of others [ 10, 6], imply that the methylation level at the 12th position of CTCF binding sequence may alter the binding environment, resulting in different zinc-finger binding and, in turn, recruiting different cofactors that ultimately leads to divergent functionalities.
P268S disturbs the backbone conformation of the linker thus interferes with nucleotide binding and may alter the affinity and hydrolysis rate of the nucleotide-binding domain.
This would then suggest that in order to monitor the DNA binding of a transcriptional complex, e.g. Hap2/Hap3/Hap4/Hap5, it would be more suitable to tag the subunits that do not bind the DNA template, speculating that tagging DNA binding subunits may alter the structure of the complex and, consequently, the affinity and the specificity of the interaction with the DNA.
Mutations M46L and I54M alter residues in the flaps and are proposed to have small indirect effects on inhibitor binding and may alter the flap dynamics.
Accumulation of premature processed profilaggrin, even if there is keratin binding activity, may alter the cubic-like, rod-packing symmetry of keratin filaments at the SG-to-SC transition and/or at the lower SC, and this may cause alteration of the SC hydration level in the SASP−/− epidermis (Norlen & Al-Amoudi, 2004).
The intrinsic stability of mRNA is determined by cis-acting sequences located within the 3′ UTR as well as trans-acting RNA-binding proteins (25); 3′ UTR variants may alter the binding of these proteins or alter the secondary structure of the 3′ UTR.
A fourth mAb with a longer CDR2 loop was not affected by mutation of residue 57, indicating that CDR2 domain length may alter the binding interface and lead to the involvement of other residues in protein A binding.
