1c94
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(New page: 200px<br /><applet load="1c94" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c94, resolution 2.08Å" /> '''REVERSING THE SEQUEN...)
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Revision as of 23:09, 24 November 2007
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REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.
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
Page seeded by OCA on Sun Nov 25 01:16:36 2007
