1c94: Difference between revisions

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[[Image:1c94.jpg|left|200px]]
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{{STRUCTURE_1c94|  PDB=1c94  |  SCENE=  }}  
{{STRUCTURE_1c94|  PDB=1c94  |  SCENE=  }}  


'''REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.'''
===REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10716989}}


==About this Structure==
==About this Structure==
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[[Category: Retro-coiled coil]]
[[Category: Retro-coiled coil]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:29:03 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:23:31 2008''

Revision as of 17:23, 30 June 2008

File:1c94.png

Template:STRUCTURE 1c94

REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.

Template:ABSTRACT PUBMED 10716989

About this Structure

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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