5EKM

Human Carbonic Anhydrase II complexed with a two-faced guest

5EKM の概要

• エントリーDOI: 10.2210/pdb5ekm/pdb
• 関連するPDBエントリー: 5EKH 5EKJ
• 分子名称: Carbonic anhydrase 2, ZINC ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: lyase-lyase inhibitor complex, lyase/lyase inhibitor
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29738.92

構造登録者

Roose, B.W.,Dmochowski, I.J. (登録日: 2015-11-03, 公開日: 2016-01-06, 最終更新日: 2024-03-06)

主引用文献

Wang, Y.,Roose, B.W.,Philbin, J.P.,Doman, J.L.,Dmochowski, I.J.
Programming A Molecular Relay for Ultrasensitive Biodetection through (129) Xe NMR.
Angew.Chem.Int.Ed.Engl., 55:1733-1736, 2016

PubMed Abstract: A supramolecular strategy for detecting specific proteins in complex media by using hyperpolarized (129) Xe NMR is reported. A cucurbit[6]uril (CB[6])-based molecular relay was programmed for three sequential equilibrium conditions by designing a two-faced guest (TFG) that initially binds CB[6] and blocks the CB[6]-Xe interaction. The protein analyte recruits the TFG and frees CB[6] for Xe binding. TFGs containing CB[6]- and carbonic anhydrase II (CAII)-binding domains were synthesized in one or two steps. X-ray crystallography confirmed TFG binding to Zn(2+) in the deep CAII active-site cleft, which precludes simultaneous CB[6] binding. The molecular relay was reprogrammed to detect avidin by using a different TFG. Finally, Xe binding by CB[6] was detected in buffer and in E. coli cultures expressing CAII through ultrasensitive (129) Xe NMR spectroscopy.

PubMed: 26692420
DOI: 10.1002/anie.201508990

実験手法

X-RAY DIFFRACTION (1.33 Å)