2nrn: Difference between revisions

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-[[Image:2nrn.gif|left|200px]]<br /><applet load="2nrn" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2nrn.gif|left|200px]]<br /><applet load="2nrn" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2nrn, resolution 1.40&Aring;" />
 '''Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant'''<br />
 ==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.
+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==
-NRN 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NRN OCA].
+NRN 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==
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 [[Category: tetramer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:52:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:07 2008''