The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure

Authors
Mittl, PRE Deillon, C Sargent, D Liu, NK Klauser, S Thomas, RM Gutte, B Grutter, MG
Citation
Pre. Mittl et al., The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure, P NAS US, 97(6), 2000, pp. 2562-2566
Citations number
35
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN journal
00278424 → ACNP
Volume
97
Issue
6
Year of publication
2000
Pages
2562 - 2566
Database
ISI
SICI code
0027-8424(20000314)97:6<2562:TRLZSF>2.0.ZU;2-J
Abstract
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-Angstrom c rystal structure of the retro-GCN4 leucine zipper. In contrast to the two-s tranded helical coiled-coil GCN4 leucine zipper, the retro-leucine zipper f ormed a very stable, parallel four-helix bundle, which now lends itself to further structural and functional studies.