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PDBsum entry 1zij

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Leucine zipper PDB id
1zij
Contents
Protein chains
34 a.a. *
Waters ×34
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystal structures of a single coiled-Coil peptide in two oligomeric states reveal the basis for structural polymorphism.
Authors L.Gonzalez, R.A.Brown, D.Richardson, T.Alber.
Ref. Nat Struct Biol, 1996, 3, 1002-1009.
PubMed id 8946853
Abstract
Each protein sequence generally adopts a single native fold, but the sequence features that confer structural uniqueness are not well understood. To define the basis for structural heterogeneity, we determined the high resolution X-ray crystal structures of a single GCN4 leucine-zipper mutant (Asn 16 to aminobutyric acid) in both dimeric and trimeric coiled-coil conformations. The mutant sequence is accommodated in two distinct structures by forming similarly-shaped packing surfaces with different sets of atoms. The trimer structure, in comparison to a previously-characterized trimeric mutant with substitutions in eight core residues, shows that the twist of individual helices and the helix-helix crossing angles can vary significantly to produce the most favoured packing arrangement.
Secondary reference #1
Title An engineered allosteric switch in leucine-Zipper oligomerization.
Authors L.Gonzalez, J.J.Plecs, T.Alber.
Ref. Nat Struct Biol, 1996, 3, 510-515.
PubMed id 8646536
Abstract
Secondary reference #2
Title Crystal structure of an isoleucine-Zipper trimer.
Authors P.B.Harbury, P.S.Kim, T.Alber.
Ref. Nature, 1994, 371, 80-83.
PubMed id 8072533
Abstract
Secondary reference #3
Title A switch between two-, Three-, And four-Stranded coiled coils in gcn4 leucine zipper mutants.
Authors P.B.Harbury, T.Zhang, P.S.Kim, T.Alber.
Ref. Science, 1993, 262, 1401-1407. [DOI no: 10.1126/science.8248779]
PubMed id 8248779
Full text Abstract
Secondary reference #4
Title X-Ray structure of the gcn4 leucine zipper, A two-Stranded, Parallel coiled coil.
Authors E.K.O'Shea, J.D.Klemm, P.S.Kim, T.Alber.
Ref. Science, 1991, 254, 539-544. [DOI no: 10.1126/science.1948029]
PubMed id 1948029
Full text Abstract
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