4DZU

Complex of 3-alpha bound to gp41-5

4DZU の概要

• エントリーDOI: 10.2210/pdb4dzu/pdb
• 関連するPDBエントリー: 3o42 4DZV
• 分子名称: gp41-5, 3-alpha, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: viral fusion, de novo protein
• 由来する生物種: Synthetic construct
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27104.18

構造登録者

Johnson, L.M.,Mortenson, D.E.,Yun, H.G.,Horne, W.S.,Ketas, T.J.,Lu, M.,Moore, J.P.,Gellman, S.H. (登録日: 2012-03-01, 公開日: 2012-05-02, 最終更新日: 2024-02-28)

主引用文献

Johnson, L.M.,Mortenson, D.E.,Yun, H.G.,Horne, W.S.,Ketas, T.J.,Lu, M.,Moore, J.P.,Gellman, S.H.
Enhancement of alpha-helix mimicry by an alpha / beta-peptide foldamer via incorporation of a dense ionic side-chain array.
J.Am.Chem.Soc., 134:7317-7320, 2012

PubMed Abstract: We report a new method for preorganization of α/β-peptide helices, based on the use of a dense array of acidic and basic side chains. Previously we have used cyclically constrained β residues to promote α/β-peptide helicity; here we show that an engineered ion pair array can be comparably effective, as indicated by mimicry of the CHR domain of HIV protein gp41. The new design is effective in biochemical and cell-based infectivity assays; however, the resulting α/β-peptide is susceptible to proteolysis. This susceptibility was addressed via introduction of a few cyclic β residues near the cleavage site, to produce the most stable, effective α/β-peptide gp41 CHR analogue identified. Crystal structures of an α- and α/β-peptide (each involved in a gp41-mimetic helix bundle) that contain the dense acid/base residue array manifest disorder in the ionic side chains, but there is little side-chain disorder in analogous α- and α/β-peptide structures with a sparser ionic side-chain array. These observations suggest that dense arrays of complementary acidic and basic residues can provide conformational stabilization via Coulombic attractions that do not require entropically costly ordering of side chains.

PubMed: 22524614
DOI: 10.1021/ja302428d

実験手法

X-RAY DIFFRACTION (2.1 Å)