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Affinity of interaction between the PDZ domain and PDZ binding domain may be higher or lower depending on surrounding sequences resulting in the specificity of interaction.
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The DNA-binding domain may be a synthetic zinc finger (ZF) or a TAL protein (TALE), which can be engineered to bind to a DNA sequence of choice.
At other genomic regions, binding to the ETS domain may be preferred by one factor over another, particularly at combined ETS-IRF elements where Spi-B is the principal partner for recruiting IRF4 to regulatory regions [ 10].
Given that the conserved DHR2 domain mediates the self-binding, dimerization through this domain may be a general mechanism for all Docks., In addition to homodimerization, heterodimerization formed between different Dock proteins (e.g., Dock1 and Dock5) is also evident.
The HTH motif is thought to mediate DNA binding, whilst the ThiJ-like domain may be an amidase, although this is unproven.
Transporters in the system will be for export (there will be no periplasmic substrate binding protein), and a protease domain may be fused to a permease subunit.
Thus in DLG5 the PDZ domain may be binding to other targets that do not require the classic GLGF motif for interaction.
We argue that the preferential structural localization of oncogenic mutations in the activation loop and the substrate binding C-lobe of the kinase domain may be determined by their strategic location critical for the kinase autoinhibition, regulation and allosteric interactions in signal transduction networks.
These data suggest that both direct DNA binding and interaction via the SAM domain may be dispensable for the regulation of certain genes.
We hypothesize that deletion of the thrombin cleavage domain may be interrupting integrin binding of OPN and therefore it could be CD44 binding to OPN which may be causing the observed effects.
Cbp peptide binding of the activation status of kinase domain may be modulated by selecting the reduced form over the oxidized form rather than directly changing the redox status of the Csk-SH2.
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