Figure 4
Figure 4. Ribbon diagram of the αIIb/β3 head region indicating possible binding footprints of 5 mAb pairs. Structural coordinates were from Protein Data Bank (3FCS)19 viewed with WebLab viewer Pro 3.7 (Molecular Simulations Inc). Amino acid residues 606-959 of αIIb and 561-690 of β3 were omitted for the sake of clarity. Alpha helical structures are red, and β sheets are turquoise. Solid ovals represent likely footprints of mAbs 10E5, 7E3, AP3, and RGD peptide based on prior crystallographic17 or mutagenic31,32 studies. Dashed ovals represent likely binding footprints of 7 other mAbs inferred from their reactions with chimeric αIIb/β3 constructs and from blocking studies summarized in Table 3.

Ribbon diagram of the αIIb3 head region indicating possible binding footprints of 5 mAb pairs. Structural coordinates were from Protein Data Bank (3FCS)19  viewed with WebLab viewer Pro 3.7 (Molecular Simulations Inc). Amino acid residues 606-959 of αIIb and 561-690 of β3 were omitted for the sake of clarity. Alpha helical structures are red, and β sheets are turquoise. Solid ovals represent likely footprints of mAbs 10E5, 7E3, AP3, and RGD peptide based on prior crystallographic17  or mutagenic31,32  studies. Dashed ovals represent likely binding footprints of 7 other mAbs inferred from their reactions with chimeric αIIb3 constructs and from blocking studies summarized in Table 3.

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