Description: Dr. Andrew Herr and colleagues at the University of Cincinnati have developed a protocol for the expression, purification, and refolding of the collagen-binding domain of human GPVI. The crystal structure of this refolded GPVI domain was solved to 2.4 Å resolution. GPVI formed a back-to-back dimer in the crystal, consistent with several studies suggesting GPVI was dimeric on the platelet surface. These data also revealed an unusual groove on the surface of GPVI that computational docking programs and published mutagenesis studies strongly suggest is the collagen binding site. The orientation and dimensions of the collagen binding grooves on the two GPVI proteins within a dimer precisely match the geometry of the intact collagen fiber.
This technology – a refolding protocol capable of generating milligram quantities of pure GPVI and the coordinates of the atomic structure of GPVI – provides critical information for the design and development of GPVI inhibitors as new therapies for human disease
US Patent # 8,084,577, entitled Crystal Structure of Human Glycoprotein VI and Applications Thereof has issued.
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