N-Terminal protein complexation and assembly with a triangular sulfated macrocycle

Ifeagwu, Marvin C., Guo, Lijuan, Mockler, Niamh M., Dong, Ming, Li, Chunju, & Crowley, Peter B. (2025). N-Terminal Protein Complexation and Assembly with a Triangular Sulfated Macrocycle. Crystal Growth & Design, 25(13), 4661-4665. https://doi.org/10.1021/acs.cgd.5c00290

Abstract

We report two cocrystal structures of a mutant Ralstonia solanacearum lectin (RSL) in complex with the recently described sulfated terphen[3]arene (STP3). This triangular macrocycle bearing 12 sulfates exhibits interesting protein-binding modes including methionine encapsulation and insertion between surface-exposed loops. These two binding modes facilitate the overall crystal packing, which may benefit from the macrocycle rigidity. In addition to a promising tool for protein assembly and crystallization, the data have implications for lectin–heparan sulfate interactions.

Funder

Research Ireland
Irish Research Council
University of Galway
National Natural Science Foundation of China
Natural Science Foundation of Tianjin City

Publisher

American Chemical Society

Rights

CC BY

cb

Collections

School of Biological and Chemical Sciences (Scholarly Articles)