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Updated: Sep 16, 2025

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
N‑Terminal Protein Complexation and Assembly with a Triangular Sulfated Macrocycle
Marvin C Ifeagwu1, Lijuan Guo2, Niamh M Mockler1
1School of Biological and Chemical Sciences, University of Galway, Galway H91 TK33, Ireland.
None:
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.
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