Download MendeleyCrystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism
Gonzalez Junior, L., Brown, R.A., Richardson, D., Alber, T.(1996) Nat Struct Biol 3: 1002-1010
- PubMed: 8946853
- DOI: https://doi.org/10.1038/nsb1296-1002
- Primary Citation of Related Structures:
1ZII, 1ZIJ - PubMed 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.
Organizational Affiliation:
Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206, USA.
