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Multivalent Calixarene Complexation of a Designed Pentameric Lectin.

Ronan J FloodLinda CerofoliniMarco FragaiPeter B Crowley
Published in: Biomacromolecules (2024)
We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene ( sclx 8 ), as characterized by X-ray crystallography and NMR spectroscopy. Two crystal structures and 15 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.
Keyphrases
  • amino acid
  • high throughput
  • genome wide
  • magnetic resonance imaging
  • computed tomography
  • dna methylation
  • dual energy
  • low density lipoprotein