4NJ2
GCN4-p1 triple Val9, 23,30 to Ile mutant
Summary for 4NJ2
Entry DOI | 10.2210/pdb4nj2/pdb |
Related | 2ZTA 4DMD 4NIZ 4NJ0 4NJ1 |
Descriptor | General control protein GCN4, GLYCEROL (3 entities in total) |
Functional Keywords | transcription |
Biological source | Saccharomyces cerevisiae (Baker's yeast) |
Cellular location | Nucleus: P03069 |
Total number of polymer chains | 2 |
Total formula weight | 8235.67 |
Authors | Oshaben, K.M.,Horne, W.S. (deposition date: 2013-11-08, release date: 2014-08-20, Last modification date: 2024-11-27) |
Primary citation | Oshaben, K.M.,Horne, W.S. Tuning assembly size in Peptide-based supramolecular polymers by modulation of subunit association affinity. Biomacromolecules, 15:1436-1442, 2014 Cited by PubMed Abstract: Nature uses proteins and nucleic acids to form a wide array of functional architectures, and scientists have found inspiration from these structures in the rational design of synthetic biomaterials. We have recently shown that a modular subunit consisting of two α-helical coiled coil peptides attached at their midpoints by an organic linking group can spontaneously self-assemble in aqueous solution to form a soluble supramolecular polymer. Here we explore the use of coiled-coil association affinity, readily tuned by amino acid sequence, as a means to predictably alter properties of these supramolecular assemblies. A series of dimeric coiled-coil peptide sequences with identical quaternary folded structures but systematically altered folded stability were designed and biophysically characterized. The sequences were cross-linked to generate a series of branched, self-assembling biomacromolecular subunits. A clear relationship is observed between coiled-coil association affinity and apparent hydrodynamic diameter of the supramolecular polymers formed by these subunits. Our results provide a family of soluble supramolecular polymers of tunable size and well-characterized coiled-coil sequences that add to the library of building blocks available for use in the rational design of protein-based supramolecular biomaterials. PubMed: 24598042DOI: 10.1021/bm5000423 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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