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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 .
One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together (dimerize) two DNA binding regions. The DNA binding region comprises a number of basic amino acids such as arginine and lysine. Proteins containing this domain are transcription factors. [1] [2]
The Protein Data Bank (PDB) is a database of 3D structure data for large biological molecules, such as proteins, DNA, and RNA. PDB is managed by an international organization called the Worldwide Protein Data Bank , which is composed of several local organizations, as. PDBe, PDBj, RCSB, and BMRB.
TRANSFAC: a database about eukaryotic transcription factors, their genomic binding sites and DNA-binding profiles; JASPAR: a database of manually curated, non-redundant transcription factor binding profiles. MetOSite: a database about methionine sulfoxidation sites and its functional roles in proteins [35]
The data in SMID is derived from the Protein Data Bank (PDB), a database of known protein crystal structures. SMID can be queried by entering a protein GI, domain identifier, PDB ID or SMID ID. The results of a search provide small molecule, protein, and domain information for each interaction identified in the database.
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 ]
Important in DNA binding proteins. Helix-turn-helix Two α helices joined by a short strand of amino acids and found in many proteins that regulate gene expression. [12] Nest Extremely common. Three consecutive amino acid residues form an anion-binding concavity. [13] Niche Extremely common.
The Protein Data Bank was announced in October 1971 in Nature New Biology [10] as a joint venture between Cambridge Crystallographic Data Centre, UK and Brookhaven National Laboratory, US. Upon Hamilton's death in 1973, Tom Koetzle took over direction of the PDB for the subsequent 20 years.