1c94
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c94]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C94 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1c94]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C94 FirstGlance]. <br> | ||
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c94 OCA], [https://pdbe.org/1c94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c94 RCSB], [https://www.ebi.ac.uk/pdbsum/1c94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c94 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c94 OCA], [https://pdbe.org/1c94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c94 RCSB], [https://www.ebi.ac.uk/pdbsum/1c94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c94 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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<ref>PMID:10716989</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1c94" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| + | *[[Gcn4 3D Structures|Gcn4 3D Structures]] | ||
*[[Gnc4 3D Structures|Gnc4 3D Structures]] | *[[Gnc4 3D Structures|Gnc4 3D Structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.
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Categories: Large Structures | Deillon CA | Gruetter MG | Gutte B | Klauser S | Liu N | Mittl PRE | Sargent D | Thomas RM
