1c94
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c94 OCA], [http://www.ebi.ac.uk/pdbsum/1c94 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c94 RCSB]</span> | ||
}} | }} | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:05 2008'' |
Revision as of 16:17, 30 March 2008
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| , resolution 2.08Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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