How do leucine zippers bind to DNA?
The bZIP interacts with the DNA via basic, amine residues (see basic amino acids in (provided table (sort by pH)) of certain amino acids in the “basic” domain, such as lysines and arginines. These basic residues interact in the major groove of the DNA, forming sequence-specific interactions.
What does a leucine zipper do?
The Leucine Zipper and the Basic DNA-Binding Domain (bZIP) The leucine zipper facilitates the dimerization of the protein by interdigitation of two leucine-containing helices on different molecules and these residues form the buried subunit interface of the coiled-coil dimer.
What holds a leucine zipper together?
Being hydrophobic, the leucines cause two adjacent alpha helices to be “zippered” together by hydrophobic interactions. On the end of each alpha helix is the DNA binding region which contains basic amino acids that form ionic bonds with the acidic DNA.
What is basic leucine zipper transcription factor?
The basic leucine zipper (bZIP) transcription factors are sequence-specific DNA-binding proteins that regulate transcription. They are characterized by a 60-80 amino acid bZIP domain: a basic DNA binding domain followed by a leucine zipper dimerization domain.
Where do leucine zippers bind?
Leucine zipper transcription factors contain leucine residues at every seventh position in the C-terminal end of the DNA-binding domains (DBDs). These proteins often function as dimers using two extended α-helices to bind DNA at two different major groves.
Where does leucine occur in protein structure?
The functional-structural role of leucine was established by showing that it occurs most frequently among residues surrounding the heme in five of the heme proteins.
What molecule is attached to leucine?
Leucine is a branched-chain amino acid that consists of glycine in which one of the hydrogens attached to the alpha-carbon is substituted by an isobutyl group.
What do DNA binding proteins do?
DNA- and RNA-binding proteins (DRBPs) constitute a significant fraction of cellular proteins and have important roles in cells. Their functions include control of transcription and translation, DNA repair, splicing, apoptosis and mediating stress responses.
How does leucine contribute to protein structure?
Role in structure: Being hydrophobic, Leucine prefers to be buried in protein hydrophobic cores. It also shows a preference for being within alpha helices more so than in beta strands.
What is leucine protein?
Leucine is one of the 3 essential branched chain amino acids (BCAAs). These amino acids can be used by skeletal muscle to give energy during exercise. Eating foods that have complete protein gives enough of these amino acids. This includes foods such as meat, poultry, fish, eggs, and milk.