1c94: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
== 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 [http://oca.weizmann.ac.il/oca-docs/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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C94 FirstGlance]. <br> | ||
</td></tr><tr><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://www.rcsb.org/pdb/explore.do?structureId=1c94 RCSB], [http://www.ebi.ac.uk/pdbsum/1c94 PDBsum]</span></td></tr> | </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://www.rcsb.org/pdb/explore.do?structureId=1c94 RCSB], [http://www.ebi.ac.uk/pdbsum/1c94 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 20: | Line 20: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Deillon, C A | [[Category: Deillon, C A]] | ||
[[Category: Gruetter, M G | [[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 R.E | [[Category: Mittl, P R.E]] | ||
[[Category: Sargent, D | [[Category: Sargent, D]] | ||
[[Category: Thomas, R M | [[Category: Thomas, R M]] | ||
[[Category: 4-alpha-helix-bundle]] | [[Category: 4-alpha-helix-bundle]] | ||
[[Category: Gene regulation]] | [[Category: Gene regulation]] | ||
[[Category: Peptide synthesis]] | [[Category: Peptide synthesis]] | ||
[[Category: Retro-coiled coil]] | [[Category: Retro-coiled coil]] |
Revision as of 13:37, 22 December 2014
REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
|