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A basic helix–loop–helix (bHLH) is a protein structural motif that characterizes one of the largest families of dimerizing transcription factors. [2][3][4][5] The word "basic" does not refer to complexity but to the chemistry of the motif because transcription factors in general contain basic amino acid residues in order to facilitate DNA ...
A DNA-binding domain (DBD) is an independently folded protein domain that contains at least one structural motif that recognizes double- or single-stranded DNA.A DBD can recognize a specific DNA sequence (a recognition sequence) or have a general affinity to DNA. [1]
CL0123. ECOD. 101.1. Helix-turn-helix is a DNA-binding domain (DBD). The helix-turn-helix (HTH) is a major structural motif capable of binding DNA. Each monomer incorporates two α helices, joined by a short strand of amino acids, that bind to the major groove of DNA. The HTH motif occurs in many proteins that regulate gene expression.
DNA-binding proteins are proteins that have DNA-binding domains and thus have a specific or general affinity for single- or double-stranded DNA. [3][4][5] Sequence-specific DNA-binding proteins generally interact with the major groove of B-DNA, because it exposes more functional groups that identify a base pair. [6][7]
Triplex DNA structure. The arrows are going from the 5' end to the 3' end. (PDB: 1BWG ) Triple-stranded DNA (also known as H-DNA or Triplex-DNA) is a DNA structure in which three oligonucleotides wind around each other and form a triple helix. In triple-stranded DNA, the third strand binds to a B-form DNA (via Watson–Crick base-pairing ...
Similar structures include the 3 10 helix (i + 3 → i hydrogen bonding) and the π-helix (i + 5 → i hydrogen bonding). The α-helix can be described as a 3.6 13 helix, since the i + 4 spacing adds three more atoms to the H-bonded loop compared to the tighter 3 10 helix, and on average, 3.6 amino acids are involved in one ring of α-helix ...
Leucine zipper. "Overhead view", or helical wheel diagram, of a leucine zipper, where d represents leucine, arranged with other amino acids on two parallel alpha helices. A leucine zipper (or leucine scissors[1]) is a common three-dimensional structural motif in proteins. They were first described by Landschulz and collaborators in 1988 [2 ...
Illustration of an activator. In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription of genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. [1][2] The function of TFs is to regulate—turn on and off—genes in order to ...