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J. Biochem, 2003, Vol. 134, No. 1 19-23
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Characterization and Preliminary Crystallographic Studies of EMS16, an Antagonist of Collagen Receptor (GPIa/IIa) from the Venom of Echis multisquamatus

Daiju Okuda1, Katsunori Horii2, Hiroshi Mizuno2 and Takashi Morita+,1

1 Department of Biochemistry, Meiji Pharmaceutical University, 2-522-1, Noshio, Kiyose, Tokyo, 204-8588; and 2 Department of Biochemistry, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602

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 {alpha}2ß1), 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 P212121, with unit-cell 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.

+ To whom correspondence should be addressed. Tel/Fax: +81-424-95-8479, E-mail: tmorita{at}my-pharm.ac.jp


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