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