1swi
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(New page: 200px<br /><applet load="1swi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1swi, resolution 2.6Å" /> '''GCN4-LEUCINE ZIPPER C...)
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Revision as of 00:40, 21 November 2007
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GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A COMPLEXED WITH BENZENE
Overview
Controversy remains about the role of core side-chain packing in, specifying protein structure. To investigate the influence of core packing, on the oligomeric structure of a coiled coil, we engineered a GCN4 leucine, zipper mutant that switches from two to three strands upon binding the, hydrophobic ligands cyclohexane and benzene. In solution these ligands, increased the apparent thermal stability and the oligomerization order of, the mutant leucine zipper. The crystal structure of the peptide-benzene, complex shows a single benzene molecule bound at the engineered site in, the core of the trimer. These results indicate that coiled coils are, well-suited to function as molecular switches and emphasize that core, packing is an important determinant of oligomerization specificity.
About this Structure
1SWI is a Single protein structure of sequence from Saccharomyces cerevisiae with BNZ as ligand. Full crystallographic information is available from OCA.
Reference
An engineered allosteric switch in leucine-zipper oligomerization., Gonzalez L Jr, Plecs JJ, Alber T, Nat Struct Biol. 1996 Jun;3(6):510-5. PMID:8646536
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