Structural Constraint of Osteopontin Facilitates Efficient Binding to CD44.

ABSTRACT: Since the original description in 1996, the interaction between the cytokine osteopontin (OPN) and the homing receptor CD44 has been extensively studied in cancer, inflammation, bone remodeling, and various other conditions. Alternative splicing and extensive posttranslational modifications by both binding partners, as well as the possibility for lateral recruitment of additional membrane receptors or soluble co-ligands into a complex have left the exact molecular requirements for high-affinity OPN-CD44 binding unresolved. We now report that there is a moderate engagement between the unmodified molecules, which results in curved double-reciprocal plots for OPN titration, suggesting the existence of two binding sites or two binding conformations. Structural constraint of OPN, by immobilizat

SUBMITTER: Fnu G 

PROVIDER: S-EPMC8228714 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature