Conserved Protein Domain Family

cl02576: B_zip1 Superfamily (this model, PSSM-Id:261357 is obsolete)
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basic leucine zipper DNA-binding and multimerization region of GCN4 and related proteins
Basic leucine zipper (bZIP) transcription factors act in networks of homo- and hetero-dimers in the regulation in a diverse set of cellular pathways. Classical leucine zippers have alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization creates a pair of basic regions that bind DNA and undergo conformational change. GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain, comprised of a basic alpha-helical DNA-binding region and a coiled-coil dimerization region.
Taxonomy: root
PubMed: 16 links
Protein: Related Protein
Related Structure
Accession: cl02576
PSSM Id: 261357
Name: B_zip1
Created: 8-Feb-2008
Updated: 16-Jan-2014
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