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One of these groups is the Dof (DNA binding with one finger) family, a particular class of zinc finger domain TFs [ 16, 17] characterized by a conserved region of 50 amino acids with a C2-C2 finger structure, associated to a basic region, that binds specifically to DNA sequences with a 5'-T/AAAAG-3' core [ 18].
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The family of transcription factors containing bZIP domain is also characterized by a basic region, which binds via hydrogen bonds to the large groove of the DNA [ 55].
Structure and function studies have shown that these transcriptional regulators act as heterodimers with the ubiquitously expressed class I bHLH E2A gene products E12 or E47; the Helix-Loop-Helix (HLH) domain mediates heterodimerisation whilst the basic region binds to a consensus E-box DNA motif in the promoter region of target genes [3,4].
Further inspection of the basic region revealed that Animals shared several moderately conserved sites with Fungi.
The LBD consists of a ligand binding pocket that binds ligand, and an activation function 2 (AF2) region that binds cofactors.
The C-terminus of Hp53 contains a basic region (9/26 residues) that can bind either DNA or RNA, and the C-terminus of Dmp53 is also relatively basic (6/24 residues).
Interestingly, the reported region that binds the Ubl includes the linker helix, which we here show binds and inhibits RING1.
Group E proteins have Pro or Gly residues within the basic region and can bind preferentially to a typical sequence, CACGNG [ 14].
Group E proteins contain Pro or Gly residues within the basic region and can bind preferentially to the CACGNG sequence [ 14, 15].
Histones are highly basic proteins that bind tightly to the acidic DNA to form chromatin.
In addition, liposome-binding assays combined with mass spectroscopy studies revealed that thrombin, a strong platelet agonist, cleaved N-PTB at a site located between the basic motifs, a region that becomes protected from thrombin cleavage when bound to sulfatides.
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