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PDBsum entry 1swi
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Leucine zipper
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PDB id
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1swi
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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An engineered allosteric switch in leucine-Zipper oligomerization.
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Authors
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L.Gonzalez,
J.J.Plecs,
T.Alber.
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Ref.
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Nat Struct Biol, 1996,
3,
510-515.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystal structure of an isoleucine-Zipper trimer.
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Authors
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P.B.Harbury,
P.S.Kim,
T.Alber.
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Ref.
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Nature, 1994,
371,
80-83.
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PubMed id
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Secondary reference #2
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Title
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A switch between two-, Three-, And four-Stranded coiled coils in gcn4 leucine zipper mutants.
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Authors
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P.B.Harbury,
T.Zhang,
P.S.Kim,
T.Alber.
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Ref.
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Science, 1993,
262,
1401-1407.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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X-Ray structure of the gcn4 leucine zipper, A two-Stranded, Parallel coiled coil.
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Authors
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E.K.O'Shea,
J.D.Klemm,
P.S.Kim,
T.Alber.
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Ref.
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Science, 1991,
254,
539-544.
[DOI no: ]
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PubMed id
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