Crystal structure of von Willebrand factor A1 domain complexed with snake venom, bitiscetin: insight into glycoprotein Ibα binding mechanism induced by snake …
N Maita, K Nishio, E Nishimoto, T Matsui… - Journal of Biological …, 2003 - ASBMB
Bitiscetin, a platelet adhesion inducer isolated from venom of the snake Bitis arietans,
activates the binding of the von Willebrand factor (VWF) A1 domain to glycoprotein Ib (GPIb)
in vitro. This activation requires the formation of a bitiscetin-VWF A1 complex, suggesting an
allosteric mechanism of action. Here, we report the crystal structure of bitiscetin-VWF A1
domain complex solved at 2.85 Å. In the complex structure, helix α5 of VWF A1 domain lies
on a concave depression on bitiscetin, and binding sites are located at both ends of the …
activates the binding of the von Willebrand factor (VWF) A1 domain to glycoprotein Ib (GPIb)
in vitro. This activation requires the formation of a bitiscetin-VWF A1 complex, suggesting an
allosteric mechanism of action. Here, we report the crystal structure of bitiscetin-VWF A1
domain complex solved at 2.85 Å. In the complex structure, helix α5 of VWF A1 domain lies
on a concave depression on bitiscetin, and binding sites are located at both ends of the …
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