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PDBsum entry 1zim

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Leucine zipper PDB id
1zim
Contents
Protein chains
33 a.a. *
Waters ×42
* Residue conservation analysis

References listed in PDB file
Key reference
Title Buried polar residues and structural specificity in the gcn4 leucine zipper.
Authors L.Gonzalez, D.N.Woolfson, T.Alber.
Ref. Nat Struct Biol, 1996, 3, 1011-1018.
PubMed id 8946854
Abstract
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.
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
PROCHECK
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