We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene (), as characterized by X-ray crystallography and NMR spectroscopy. Two crystal structures and 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 complex, with the largest protein-calixarene interface observed to date. This system provides a platform for investigating multivalency.
We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene (), as characterized by X-ray crystallography and NMR spectroscopy. Two crystal structures and 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 complex, with the largest protein-calixarene interface observed to date. This system provides a platform for investigating multivalency.
