Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant.

doi:10.1110/ps.062590807

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Article

Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant.

Protein science : a publication of the Protein Society - 1 Feb 2007

Deng Yiqun, Zheng Qi, Liu Jie, Cheng Chao-Sheng, Kallenbach Neville R, Lu Min

Abstract excerpt

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...

Topics

Crystallography, X-Ray
Dimerization
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Leucine Zippers
Models, Molecular
Mutant Proteins
Mutation
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary

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Identifiers

PMID: 17189475
DOI: 10.1110/ps.062590807
PMCID: PMC2203300

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