Version 2 2024-01-16, 19:34Version 2 2024-01-16, 19:34
Version 1 2024-01-16, 17:06Version 1 2024-01-16, 17:06
journal contribution
posted on 2024-01-16, 19:34authored byRonan
J. Flood, Linda Cerofolini, Marco Fragai, Peter B. Crowley
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.