Identification of the primary collagen-binding surface on human glycoprotein VI by site-directed mutagenesis and by a blocking phage antibody.

@article{Smethurst2004IdentificationOT,
  title={Identification of the primary collagen-binding surface on human glycoprotein VI by site-directed mutagenesis and by a blocking phage antibody.},
  author={Peter A. Smethurst and Lotta Joutsi-Korhonen and Marie O'connor and Erica Wilson and Nicola S. Jennings and Stephen Garner and Yanjun Zhang and C. Graham Knight and Timothy R. Dafforn and Ashley M. Buckle and Martin J W Ijsseldijk and Philip G. de Groot and Nicholas A. Watkins and Richard W Farndale and Willem H Ouwehand},
  journal={Blood},
  year={2004},
  volume={103 3},
  pages={903-11}
}
Glycoprotein (GP) VI is the major receptor responsible for platelet activation by collagen, but the collagen-binding surface of GPVI is unknown. To address this issue we expressed, from insect cells, the immunoglobulin (Ig)-like ectodomains (residues 1-185) of human and murine GPVI, called hD1D2 and mD1D2, respectively. Both proteins bound specifically to collagen-related peptide (CRP), a GPVI-specific ligand, but hD1D2 bound CRP more strongly than did mD1D2. Molecular modeling and sequence… CONTINUE READING

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