title: CHIPS binds to the phosphorylated N-terminus of the C5a-receptor.
abstract: Replacement of the sulfate groups, present in vivo on the N-terminus of the C5a-receptor (C5aR), by phosphate groups is explored. Phosphorylated mimics of the C5a-receptor N-terminus are synthesized and their binding to Chemotaxis Inhibitory Protein of Staphylococcus aureus (CHIPS) is studied by ITC and NMR. The phosphorylated C5aR mimics showed comparable binding affinity and a similar binding mode towards CHIPS compared to their sulfated forms. The activities of the phosphorylated peptides in a biological assay, however, were significantly lower compared to their sulfated counterparts.
authors.affiliation: Medicinal Chemistry & Chemical Biology, Faculty of Science, Utrecht University, Sorbonnelaan 16, 3584 CA, Utrecht, The Netherlands.
authors.forename: Anton
authors.initials: A
authors.lastname: Bunschoten
authors.forename: Louris J
authors.initials: LJ
authors.lastname: Feitsma
authors.forename: John A W
authors.initials: JA
authors.lastname: Kruijtzer
authors.forename: Carla J C
authors.initials: CJ
authors.lastname: de Haas
authors.forename: Rob M J
authors.initials: RM
authors.lastname: Liskamp
authors.forename: Johan
authors.initials: J
authors.lastname: Kemmink
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D018716:Molecular Mimicry; D010766:Phosphorylation; D011485:Protein Binding; D044087:Receptor, Anaphylatoxin C5a / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D044087:Receptor, Anaphylatoxin C5a; C493134:chemotaxis inhibitory protein, Staphylococcus aureus