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4NJ1

GCN4-p1 double Val9, 23 to Ile mutant

Summary for 4NJ1
Entry DOI10.2210/pdb4nj1/pdb
Related2ZTA 4DMD 4NIZ 4NJ0 4NJ2
DescriptorGeneral control protein GCN4 (2 entities in total)
Functional Keywordstranscription
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
Cellular locationNucleus: P03069
Total number of polymer chains2
Total formula weight8115.53
Authors
Oshaben, K.M.,Horne, W.S. (deposition date: 2013-11-08, release date: 2014-08-20, Last modification date: 2023-09-20)
Primary citationOshaben, 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: 24598042
DOI: 10.1021/bm5000423
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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数据于2024-11-13公开中

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