TheBasic Leucine Zipper Domain (bZIP domain) is found in manyDNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and theleucine zipper that is required to hold together (dimerize) two DNA binding regions. The DNA binding region comprises a number of basic amino acids such asarginine andlysine. Proteins containing this domain aretranscription factors.[1][2]
bZIP transcription factors are found in all eukaryotes and form one of the largest families of dimerizing TFs.[3] An evolutionary study from 2008 revealed that 4 bZIP genes were encoded by the genome of themost recent common ancestor of all plants.[4] Interactions between bZIP transcription factors are numerous and complex[5][6][3] and play important roles in cancer development[7] in epithelial tissues, steroid hormone synthesis by cells of endocrine tissues,[8] factors affecting reproductive functions,[9] and several other phenomena that affect human health.
^Ellenberger T (1994). "Getting a grip in DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains".Curr. Opin. Struct. Biol.4 (1):12–21.doi:10.1016/S0959-440X(94)90054-X.
^Hurst HC (1995). "Transcription factors 1: bZIP proteins".Protein Profile.2 (2):101–68.PMID7780801.
^abAmoutzias, Grigoris D.; Robertson, David L.; Van de Peer, Yves; Oliver, Stephen G. (2008-05-01). "Choose your partners: dimerization in eukaryotic transcription factors".Trends in Biochemical Sciences.33 (5):220–229.doi:10.1016/j.tibs.2008.02.002.ISSN0968-0004.PMID18406148.
^Vlahopoulos SA, Logotheti S, Mikas D, Giarika A, Gorgoulis V, Zoumpourlis V (April 2008). "The role of ATF-2 in oncogenesis".BioEssays.30 (4):314–27.doi:10.1002/bies.20734.PMID18348191.S2CID678541.
