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Updated: Jan 27, 2026

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
Published on: July 2, 2010
Selective recognition of choline phosphate by tripodal hexa-urea receptors with dual binding sites: crystal and
Wei Zuo1, Chuandong Jia1, Huizheng Zhang1
1Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education , College of Chemistry and Materials Science , Northwest University , Xi'an 710069 , China . Email: yangxiaojuan@nwu.edu.cn ;
Abstract:
Two tripodal hexa-urea receptors functionalized with aromatic terminal groups are capable of binding choline phosphate (CP). Crystal structures of the host-guest complexes reveal that the zwitterion CP is efficiently encapsulated in the tripodal hosts in a dual-site binding mode. The phosphate tail of CP is coordinated by the urea groups and the quaternary ammonium head is bound in a 'composite aromatic box' through cation-π and hydrogen-bonding interactions. Such a partial aromatic binding environment for the Me3N-+ cation mimics that of most enzymes catalyzing the conversion of quaternary ammonium substrates. Moreover, NMR, ESI-MS, and fluorescence studies demonstrate the selective binding and sensing of CP over other competing species such as ADP, ATP, choline and derivatives.
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