1c94
From Proteopedia
(Difference between revisions)
(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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| - | [[Image:1c94.jpg|left|200px]]<br /><applet load="1c94" size=" | + | [[Image:1c94.jpg|left|200px]]<br /><applet load="1c94" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c94, resolution 2.08Å" /> | caption="1c94, resolution 2.08Å" /> | ||
'''REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.'''<br /> | '''REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The question of whether a protein whose natural sequence is inverted | + | 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== | ==About this Structure== | ||
| - | 1C94 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1C94 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10716989 10716989] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Deillon, C | + | [[Category: Deillon, C A.]] |
| - | [[Category: Gruetter, M | + | [[Category: Gruetter, M G.]] |
[[Category: Gutte, B.]] | [[Category: Gutte, B.]] | ||
[[Category: Klauser, S.]] | [[Category: Klauser, S.]] | ||
[[Category: Liu, N.]] | [[Category: Liu, N.]] | ||
| - | [[Category: Mittl, P | + | [[Category: Mittl, P R.E.]] |
[[Category: Sargent, D.]] | [[Category: Sargent, D.]] | ||
| - | [[Category: Thomas, R | + | [[Category: Thomas, R M.]] |
[[Category: 4-alpha-helix-bundle]] | [[Category: 4-alpha-helix-bundle]] | ||
[[Category: peptide synthesis]] | [[Category: peptide synthesis]] | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:41 2008'' |
Revision as of 10:03, 21 February 2008
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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 Thu Feb 21 12:03:41 2008
