4NJ2

GCN4-p1 triple Val9, 23,30 to Ile mutant

4NJ2 の概要

• エントリーDOI: 10.2210/pdb4nj2/pdb
• 関連するPDBエントリー: 2ZTA 4DMD 4NIZ 4NJ0 4NJ1
• 分子名称: General control protein GCN4, GLYCEROL (3 entities in total)
• 機能のキーワード: transcription
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Nucleus: P03069
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8235.67

構造登録者

Oshaben, K.M.,Horne, W.S. (登録日: 2013-11-08, 公開日: 2014-08-20, 最終更新日: 2024-11-27)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.2 Å)