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The PD is composed of a bipartite DNA binding domain that consists of two helix-turn-helix motifs, the PAI and the RED subdomains.
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Compared with ZFNs harboring a DNA-binding domain that consists of three to four zinc fingers, TALENs have three advantages in targeted mutagenesis: (1) DNA binding specificity is higher, (2) off-target effects are lower, and (3) construction of DNA-binding domains is easier (Pan et al., 2013).
30 33 One of the defining features of WRKY TFs is their DNA binding region, also called WRKY domain, that consists of about 60 amino acids, characterized by the highly conserved WRKY signature at the N-terminus adjacent to an atypical, either Cx4 5Cx22 23HXH or Cx7Cx23HXC, zinc-finger motif at the C-terminus.
The N-terminus includes a Flavodoxin-like domain that consists of about 170 residues with a flavin mononucleotide (FMN -binding site.
The receptors contain extracellular domains, including a ligand-binding domain, a cysteine-rich domain, two fibronectin type III repeats, and an intracellular cytoplasmic domain that consists of a juxtamembrane region, a tyrosine kinase domain, a sterile alpha motif (SAM), and a C-terminal PSD95/Discs large/Zona Occludens 1 protein (PDZ binding motif [30].
Structurally, PTPN22 consists of two functional domains: the N-terminal catalytic-dephosphorylation domain and the C-terminal binding domain that mediates its interaction with the SH3 domain of the intracellular C-src tyrosine kinase (CSK) [ 39].
The second generation of thrombolytics was produced with the help of genetic engineering, consists of fibrin binding domains that target the activation of plasminogen and thereby fibrin clot degradation.
They consist of a central DNA-binding domain that directs the receptor to specific DNA sequences within a gene promoter, and a ligand-binding domain, which can accommodate a variety of different compounds.
This protein consists of a flavodoxin-like FMN-binding domain that is connected to a cytochrome p450 reductase-like domain, including a FAD binding pocket and an NADP(H) binding site (Fig. S5).
Calmodulin is a calcium binding protein that consists of four EF-hand domains.
The protein structure can be separated into two domains: a small N-terminal ATP-binding domain consisting of five β-sheets and one α-helix (αC) and a larger C-terminal substrate-binding domain that is predominantly helical [ 21, 22].
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