5N10

Cucurbit[8]uril and 14-3-3 based binary bivalent supramolecular-protein assembly platform

5N10 の概要

• エントリーDOI: 10.2210/pdb5n10/pdb
• 分子名称: Estrogen receptor, 14-3-3 protein beta/alpha, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: supramolecular complex, scaffold protein, host-guest, transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 62519.83

構造登録者

de Vink, P.J.,Ottmann, C. (登録日: 2017-02-04, 公開日: 2017-05-24, 最終更新日: 2024-11-06)

主引用文献

de Vink, P.J.,Briels, J.M.,Schrader, T.,Milroy, L.G.,Brunsveld, L.,Ottmann, C.
A Binary Bivalent Supramolecular Assembly Platform Based on Cucurbit[8]uril and Dimeric Adapter Protein 14-3-3.
Angew. Chem. Int. Ed. Engl., 56:8998-9002, 2017

PubMed Abstract: Interactions between proteins frequently involve recognition sequences based on multivalent binding events. Dimeric 14-3-3 adapter proteins are a prominent example and typically bind partner proteins in a phosphorylation-dependent mono- or bivalent manner. Herein we describe the development of a cucurbit[8]uril (Q8)-based supramolecular system, which in conjunction with the 14-3-3 protein dimer acts as a binary and bivalent protein assembly platform. We fused the phenylalanine-glycine-glycine (FGG) tripeptide motif to the N-terminus of the 14-3-3-binding epitope of the estrogen receptor α (ERα) for selective binding to Q8. Q8-induced dimerization of the ERα epitope augmented its affinity towards 14-3-3 through a binary bivalent binding mode. The crystal structure of the Q8-induced ternary complex revealed molecular insight into the multiple supramolecular interactions between the protein, the peptide, and Q8.

PubMed: 28510303
DOI: 10.1002/anie.201701807

実験手法

X-RAY DIFFRACTION (1.6 Å)