Title : A platform of C-type lectin-like receptor
CLEC-2 for binding O-glycosylated
podoplanin and nonglycosylated
rhodocytin
Abstract :
- Podoplanin is a transmembrane O-glycoprotein that binds to C-type lectin-like receptor 2 2 (CLEC-2 )
- The O-glycan-dependent interaction seems to play crucial roles in various biological processes, such as platelet aggregation
- Rhodocytin , a snake venom, also binds to CLEC-2 and aggregates platelets in a glycan-independent manner
- To elucidate the structural basis of the glycan-dependent and independent interactions, we performed comparative crystallographic studies of podoplanin and rhodocytin in complex with CLEC-2
- Both podoplanin and rhodocytin bind to the noncanonical "side" face of CLEC-2
- There is a common interaction mode between consecutive acidic residues on the ligands and the same arginine residues on CLEC-2
- Other interactions are ligand-specific
- Carboxyl groups from the sialic acid residue on podoplanin and from the C terminus of the rhodocytin α subunit interact differently at this "second" binding site on CLEC-2
- The unique and versatile binding modes open a way to understand the functional consequences of CLEC-2-ligand interactions
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. O-glycosylated, , podoplanin, -, -
- 0. nonglycosylated, , rhodocytin, -, -
- 1. O-glycoprotein, , O-glycoprotein, -, -
- 1. O-glycoprotein, , Podoplanin, -, -
- 8. residue, , podoplanin, residue, -
Output(Part-Of) (sent_index,
protein,
site):
- 5. CLEC-2, face
- 6. CLEC-2, arginine residues
- 6. CLEC-2, residues
- 8. CLEC-2, site
- 8. subunit, terminus
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):