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1c94

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{{STRUCTURE_1c94| PDB=1c94 | SCENE= }}
{{STRUCTURE_1c94| PDB=1c94 | SCENE= }}
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'''REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.'''
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===REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 10716989 is the PubMed ID number.
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:29:03 2008''
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''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

Image: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

Page seeded by OCA on Mon Jun 30 20:23:31 2008

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