4NCV

Foldon domain wild type N-conjugate

4NCV の概要

• エントリーDOI: 10.2210/pdb4ncv/pdb
• 関連するPDBエントリー: 1FRO 4NCU 4NCW
• 分子名称: Fibritin (2 entities in total)
• 機能のキーワード: trimeric scaffold, chemical ligation, folding, trazido-functionalized trimesic acid scaffold, viral protein
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 9331.50

構造登録者

Graewert, M.A.,Berthelmann, A.,Lach, J.,Groll, M.,Eichler, J. (登録日: 2013-10-25, 公開日: 2014-03-12, 最終更新日: 2024-11-06)

主引用文献

Berthelmann, A.,Lach, J.,Grawert, M.A.,Groll, M.,Eichler, J.
Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer.
Org.Biomol.Chem., 12:2606-2614, 2014

PubMed Abstract: C3-Symmetric trimesic acid scaffolds, functionalized with bromoacetyl, aminooxyacetyl and azidoacetyl moieties, respectively, were synthesized and compared regarding their utility for the trivalent presentation of peptides using three different chemoselective ligation reactions, i.e. thioether and oxime formation, as well as the "click" reaction. The latter ligation method was then used to covalently stabilize the trimer of foldon, a 27 amino acid trimerization domain of bacteriophage T4 fibritin, by linking the three foldon monomers to the triazido-functionalized trimesic acid scaffold. This reaction dramatically enhanced the thermal stability of the trimer, while maintaining the correct fold, as demonstrated by CD spectroscopy and X-ray crystal structure analysis, respectively, of the foldon-scaffold conjugates.

PubMed: 24637609
DOI: 10.1039/c3ob42251h

実験手法

X-RAY DIFFRACTION (1.2 Å)