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Multivalent Calixarene Complexation of a Designed Pentameric Lectin.


ABSTRACT: We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene (sclx8), as characterized by X-ray crystallography and NMR spectroscopy. Two crystal structures and 15N HSQC experiments reveal a single calixarene binding site in the concave pocket of the β-propeller toroid. Despite the symmetry mismatch between the pentameric protein and the octameric macrocycle, they form a high affinity multivalent complex, with the largest protein-calixarene interface observed to date. This system provides a platform for investigating multivalency.

SUBMITTER: Flood RJ 

PROVIDER: S-EPMC10865345 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature

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Multivalent Calixarene Complexation of a Designed Pentameric Lectin.

Flood Ronan J RJ   Cerofolini Linda L   Fragai Marco M   Crowley Peter B PB  

Biomacromolecules 20240116 2


We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene (<b>sclx</b><sub><b>8</b></sub>), as characterized by X-ray crystallography and NMR spectroscopy. Two crystal structures and <sup>15</sup>N HSQC experiments reveal a single calixarene binding site in the concave pocket of the β-propeller toroid. Despite the symmetry mismatch between the pentameric protein and the octameric macrocycle, they form a high affinity multivalent co  ...[more]

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