2nrn
From Proteopedia
(New page: 200px<br /><applet load="2nrn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nrn, resolution 1.40Å" /> '''Self-assembly of coi...) |
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| - | [[Image:2nrn.gif|left|200px]]<br /><applet load="2nrn" size=" | + | [[Image:2nrn.gif|left|200px]]<br /><applet load="2nrn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2nrn, resolution 1.40Å" /> | caption="2nrn, resolution 1.40Å" /> | ||
'''Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant'''<br /> | '''Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The hydrophobic core of the GCN4 leucine-zipper dimerization domain is | + | The hydrophobic core of the GCN4 leucine-zipper dimerization domain is formed by a parallel helical association between nonpolar side chains at the a and d positions of the heptad repeat. Here we report a self-assembling coiled-coil array formed by the GCN4-pAe peptide that differs from the wild-type GCN4 leucine zipper by alanine substitutions at three charged e positions. GCN4-pAe is incompletely folded in normal solution conditions yet self-assembles into an antiparallel tetraplex in crystals by formation of unanticipated hydrophobic seams linking the last two heptads of two parallel double-stranded coiled coils. The GCN4-pAe tetramers in the lattice associate laterally through the identical interactions to those in the intramolecular dimer-dimer interface. The van der Waals packing interaction in the solid state controls extended supramolecular assembly of the protein, providing an unusual atomic scale view of a mesostructure. |
==About this Structure== | ==About this Structure== | ||
| - | 2NRN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2NRN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:07 2008'' |
Revision as of 16:10, 21 February 2008
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Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant
Overview
The hydrophobic core of the GCN4 leucine-zipper dimerization domain is formed by a parallel helical association between nonpolar side chains at the a and d positions of the heptad repeat. Here we report a self-assembling coiled-coil array formed by the GCN4-pAe peptide that differs from the wild-type GCN4 leucine zipper by alanine substitutions at three charged e positions. GCN4-pAe is incompletely folded in normal solution conditions yet self-assembles into an antiparallel tetraplex in crystals by formation of unanticipated hydrophobic seams linking the last two heptads of two parallel double-stranded coiled coils. The GCN4-pAe tetramers in the lattice associate laterally through the identical interactions to those in the intramolecular dimer-dimer interface. The van der Waals packing interaction in the solid state controls extended supramolecular assembly of the protein, providing an unusual atomic scale view of a mesostructure.
About this Structure
2NRN is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant., Deng Y, Zheng Q, Liu J, Cheng CS, Kallenbach NR, Lu M, Protein Sci. 2007 Feb;16(2):323-8. Epub 2006 Dec 22. PMID:17189475
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