Site of interaction of GPVI with Nb2 and CRP. (A) Enlarged view of the GPVI–Nb2 binding interface. GPVI is colored in light green, and Nb2 binding residues in the CDR3 loop are colored in blue and non-CDR3 residues in pink. Red dashed lines indicate polar contacts made between GPVI and Nb2 residues. The full CDR3 sequence for Nb2 is provided underneath the structure with binding residues highlighted in bold. (B) Enlarged view of the CRP binding groove of the CRP-bound GPVI structure (pink) and Nb-bound structure (green), with CRP shown in cyan and Nb2 cdr3 residues 100 to 105 shown in blue. The binding of Nb2 toward the top of the binding groove results in a shift of the βC′ sheet, resulting in a small distortion of the CRP binding groove. (C) Locations of the known Nb2 and CRP binding sites on GPVI. (i) Surface representation of Nb2 (pink) modeled onto the GPVI–CRP complex structure (PDB: 5OU8), colored in green and cyan, respectively, revealing the 2 nonoverlapping but closely situated binding sites. (ii) Nb2 and CRP binding residues mapped as pink and cyan spheres, respectively, on the structure of GPVI.