The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Characterization and Preliminary Crystallographic Studies of EMS 16, an Antagonist of Collagen Receptor (GPIa/IIa) from the Venom of Echis multisquamatus
Daiju OkudaKatsunori HoriiHiroshi MizunoTakashi Morita
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2003 年 134 巻 1 号 p. 19-23

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EMS 16 is a member of the snake venom-derived C-type lectin family of proteins (CLPs) found in the venom of Echis multisquamatus. It binds to glycoprotein Ia/IIa (integrin α2β1), a major collagen receptor of platelets, acting as a potent antagonist of platelet aggregation and cell migration. Amino acid sequencing and cDNA cloning of EMS 16 have revealed that it is composed of an A chain of 134 amino acid residues and a B chain of 128 residues. Crystals of EMS 16 belong to space group P212121, with unitcell parameters a=46.57, b=59.93, and c=115.74 Å, and diffract to a resolution of 1.9 Å. Phase determination is underway by means of molecular replacement with the structure of blood coagulation factor IX-binding protein (IX-bp) from habu snake venom (PDB code 1bj3) as the search model.
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