Open AccessThe retro -GCN4 leucine zipper sequence forms a stable three-dimensional structure
Author(s) -
Peer R. E. Mittl,
Christine Deillon,
David F. Sargent,
Niankun Liu,
Stephan Klauser,
Richard M. Thomas,
Bernd Gutte,
Markus G. Grütter
Publication year - 2000
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.97.6.2562
Subject(s) - leucine zipper , zipper , coiled coil , bzip domain , basic helix loop helix leucine zipper transcription factors , leucine , helix (gastropod) , sequence (biology) , atf3 , crystallography , protein structure , bundle , helix bundle , chemistry , biology , peptide sequence , biochemistry , amino acid , materials science , dna binding protein , transcription factor , mathematics , ecology , gene expression , promoter , algorithm , snail , composite material , gene
The question of whether a protein whose natural sequence is inverted adopts a stable fold is still under debate. We have determined the 2. 1-A crystal structure of the retro-GCN4 leucine zipper. In contrast to the two-stranded helical coiled-coil GCN4 leucine zipper, the retro-leucine zipper formed a very stable, parallel four-helix bundle, which now lends itself to further structural and functional studies.