When Mr. Haywood and colleagues compared the binding features of OSCAR with previously published protein/CLP crystal structures, their review suggested that OSCAR has complex modes of collagen recognition. This analysis was reinforced by the team’s functional characterization of the OSCAR residues. Their experiments revealed that the Phe pocket is less important for OSCAR recognition of collagen I than it is for CLP. The unexpected result provides an explanation for why the collagen motif from surfactant protein D is able to bind to OSCAR and result in cellular signaling. The investigators concluded their research by reporting that a CLP peptide required a length of 40 amino acids to inhibit osteoclastogenesis in vitro.
Lara C. Pullen, PhD, is a medical writer based in the Chicago area.
Reference
- Haywood J, Qi J, Chen CC, et al. Structural basis of collagen recognition by human osteoclast-associated receptor and design of osteoclastogenesis inhibitors. Proc Natl Acad Sci USA. 2016 Jan 7. pii: 201522572. [Epub ahead of print]