1c94: 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]] 2.08&#8491;</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.
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>
From MEDLINE&reg;/PubMed&reg;, 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>

Latest revision as of 06:41, 7 February 2024

REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.

1c94, resolution 2.08Å

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