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PDBsum entry 1zim
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Leucine zipper
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PDB id
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1zim
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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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Buried polar residues and structural specificity in the gcn4 leucine zipper.
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Authors
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L.Gonzalez,
D.N.Woolfson,
T.Alber.
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Ref.
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Nat Struct Biol, 1996,
3,
1011-1018.
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PubMed id
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Abstract
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A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine
zipper selectively favours the parallel, dimeric, coiled-coil structure. To test
if other polar residues confer oligomerization specificity, the structural
effects of Gln and Lys substitutions for Asn 16 were characterized. Like the
wild-type peptide, the Asn 16Lys mutant formed exclusively dimers. In contrast,
Gln 16, despite its chemical similarity to Asn, allowed the peptide to form both
dimers and trimers. The Gln 16 side chain was accommodated by qualitatively
different interactions in the dimer and trimer crystal structures. These
findings demonstrate that the structural selectivity of polar residues results
not only from the burial of polar atoms, but also depends on the complementarity
of the side-chain stereochemistry with the surrounding structural environment.
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Secondary reference #1
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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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Secondary reference #2
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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 #3
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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 #4
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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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