1c94 | pdb_00001c94
REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.
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| 1c94, resolution 2.08Å | |||||||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1C94 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure., Mittl PR, Deillon C, Sargent D, Liu N, Klauser S, Thomas RM, Gutte B, Grutter MG, Proc Natl Acad Sci U S A. 2000 Mar 14;97(6):2562-6. PMID:10716989
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