1c94

<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 [http://oca.weizmann.ac.il/oca-docs/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'>[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://pdbe.org/1c94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c94 RCSB], [http://www.ebi.ac.uk/pdbsum/1c94 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c94 ProSAT]</span></td></tr>

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== 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>

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<div class="pdbe-citations 1c94" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Deillon, C A]]

[[Category: Gruetter, M G]]

[[Category: Gutte, B]]

[[Category: Klauser, S]]

[[Category: Liu, N]]

[[Category: Mittl, P R.E]]

[[Category: Sargent, D]]

[[Category: Thomas, R M]]

[[Category: Retro-coiled coil]]