Search results
Results From The WOW.Com Content Network
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 ]
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 .
The TALE domain responsible for binding to DNA is known to have 1.5 to 33.5 short sequences that are repeated multiple times (tandem repeats). [2] Each of these repeats was found to be specific for a certain base pair of the DNA. [2] These repeats also have repeat variable residues (RVD) that can detect specific DNA base pairs. [2]
Oligodendrocyte transcription factor (OLIG2) is a basic helix-loop-helix transcription factor encoded by the OLIG2 gene. The protein is of 329 amino acids in length, 32 kDa in size and contains one basic helix-loop-helix DNA-binding domain. [5]
First, it has an ARID domain, which is a DNA-binding domain that can specifically bind an AT-rich DNA sequence known to be recognized by a SWI/SNF complex at the beta-globin locus. Second, the C-terminus of the protein can stimulate glucocorticoid receptor -dependent transcriptional activation.
As well as DNA-binding functions, evidence suggests that the ETS domain is also involved in protein-protein interactions. There is limited similarity outside the ETS DNA binding domain. Other domains are also present and vary from ETS member to ETS member, including the Pointed domain, a subclass of the SAM domain family.
In molecular biology, binding domain is a protein domain which binds to a specific atom or molecule, such as calcium or DNA. A protein domain is a part of a protein sequence and a tertiary structure that can change or evolve, function, and live by itself independent of the rest of the protein chain. [1] Upon binding, proteins may undergo a ...
In general, transcription factors (including this type) are dimeric, each with one helix containing basic amino acid residues that facilitate DNA binding. [6] In general, one helix is smaller, and due to the flexibility of this loop, allows dimerization by folding and packing against another helix.