2LDC

Solution structure of the estrogen receptor-binding stapled peptide SP1 (Ac-HXILHXLLQDS-NH2)

2LDC の概要

• エントリーDOI: 10.2210/pdb2ldc/pdb
• 関連するPDBエントリー: 2LDA 2LDD
• NMR情報: BMRB: 17658
• 分子名称: Estrogen receptor-binding stapled peptide SP1 (1 entity in total)
• 機能のキーワード: de novo protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1355.65

構造登録者

Phillips, C.,Bazin, R.,Bent, A.,Davies, N.,Moore, R.,Pannifer, A.,Pickford, A.,Prior, S.,Read, C.,Roberts, L.,Schade, M.,Scott, A.,Brown, D.,Xu, B.,Irving, S. (登録日: 2011-05-20, 公開日: 2011-07-06, 最終更新日: 2024-11-20)

主引用文献

Phillips, C.,Roberts, L.R.,Schade, M.,Bazin, R.,Bent, A.,Davies, N.L.,Moore, R.,Pannifer, A.D.,Pickford, A.R.,Prior, S.H.,Read, C.M.,Scott, A.,Brown, D.G.,Xu, B.,Irving, S.L.
Design and structure of stapled peptides binding to estrogen receptors.
J.Am.Chem.Soc., 133:9696-9699, 2011

PubMed Abstract: Synthetic peptides that specifically bind nuclear hormone receptors offer an alternative approach to small molecules for the modulation of receptor signaling and subsequent gene expression. Here we describe the design of a series of novel stapled peptides that bind the coactivator peptide site of estrogen receptors. Using a number of biophysical techniques, including crystal structure analysis of receptor-stapled peptide complexes, we describe in detail the molecular interactions and demonstrate that all-hydrocarbon staples modulate molecular recognition events. The findings have implications for the design of stapled peptides in general.

PubMed: 21612236
DOI: 10.1021/ja202946k

実験手法

SOLUTION NMR