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Title
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Characterization and preliminary crystallographic studies of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus.
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Authors
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D.Okuda,
K.Horii,
H.Mizuno,
T.Morita.
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Ref.
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J Biochem (tokyo), 2003,
134,
19-23.
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PubMed id
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Abstract
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EMS16 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 alpha2beta1), a major collagen receptor of platelets, acting as
a potent antagonist of platelet aggregation and cell migration. Amino acid
sequencing and cDNA cloning of EMS16 have revealed that it is composed of an A
chain of 134 amino acid residues and a B chain of 128 residues. Crystals of
EMS16 belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.57,
b = 59.93, and c = 115.74 A, and diffract to a resolution of 1.9 A. 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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