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.
| Original language | English |
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| Pages (from-to) | 1303-1309 |
| Number of pages | 7 |
| Journal | Biomacromolecules |
| Volume | 25 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 12 Feb 2024 |