1gcl
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==GCN4 LEUCINE ZIPPER CORE MUTANT P-LI== | |
| - | + | <StructureSection load='1gcl' size='340' side='right' caption='[[1gcl]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[1gcl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCL FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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=1gcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gcl RCSB], [http://www.ebi.ac.uk/pdbsum/1gcl PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold. | ||
| - | + | A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.,Harbury PB, Zhang T, Kim PS, Alber T Science. 1993 Nov 26;262(5138):1401-7. PMID:8248779<ref>PMID:8248779</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
==See Also== | ==See Also== | ||
*[[Gcn4|Gcn4]] | *[[Gcn4|Gcn4]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Alber, T | + | [[Category: Alber, T]] |
| - | [[Category: Harbury, P B | + | [[Category: Harbury, P B]] |
| - | [[Category: Kim, P S | + | [[Category: Kim, P S]] |
| - | [[Category: Zhang, T | + | [[Category: Zhang, T]] |
[[Category: Hydrophobic core mutant]] | [[Category: Hydrophobic core mutant]] | ||
[[Category: Leucine zipper]] | [[Category: Leucine zipper]] | ||
Revision as of 12:48, 18 December 2014
GCN4 LEUCINE ZIPPER CORE MUTANT P-LI
| |||||||||||
