The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
摘要：
A 30 amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein. Display of these respective amino acid sequences on an idealized .alpha. helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eighty helical turns. The periodic array of at least four leucines was also noted in the sequences of the Fos and Jun transforming proteins, as well as that of the yeast gene regulatory protein, GCN4. The polypeptide segments containing these periodic arrays of leucine residues are proposed to exist in an .alpha.-helical conformation, and the leucine side chains extending from one .alpha. helix interdigitate with those displayed from a similar .alpha. helix of a second polypeptide, facilitating dimerization. This hypothetical structure is referred to as the "leucine zipper", and it may represent a characteristic property of a new category of DNA binding proteins.
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关键词：
DNA-Binding Proteins Proto-Oncogene Proteins Protein Conformation Binding Sites Computer Simulation Leucine Enhancer Elements, Genetic Models, Molecular Structure-Activity Relationship
DOI：
10.1126/science.3289117
被引量：
年份：
1988
BMJ
Wiley
万方医学
Semantic Scholar
dx.doi.org
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