1c94
From Proteopedia
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[[Image:1c94.jpg|left|200px]] | [[Image:1c94.jpg|left|200px]] | ||
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'''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.''' | ||
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==About this Structure== | ==About this Structure== | ||
- | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C94 OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/10716989 10716989] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10716989 10716989] | ||
- | [[Category: Protein complex]] | ||
[[Category: Deillon, C A.]] | [[Category: Deillon, C A.]] | ||
[[Category: Gruetter, M G.]] | [[Category: Gruetter, M G.]] | ||
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[[Category: Thomas, R M.]] | [[Category: Thomas, R M.]] | ||
[[Category: 4-alpha-helix-bundle]] | [[Category: 4-alpha-helix-bundle]] | ||
- | [[Category: | + | [[Category: Peptide synthesis]] |
- | [[Category: | + | [[Category: Retro-coiled coil]] |
- | [[Category: | + | [[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 | + |
Revision as of 09:29, 2 May 2008
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
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 Fri May 2 12:29:03 2008