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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism.

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.[1]

References

  1. Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism. Gonzalez, L., Brown, R.A., Richardson, D., Alber, T. Nat. Struct. Biol. (1996) [Pubmed]
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