Purification, crystallization and preliminary X-ray crystallographic analysis of agkaggregin, a C-type lectin-like protein from Agkistrodon acutus venom.
A snake-venom C-type lectin-like protein, agkaggregin, has been isolated from Agkistrodon acutus venom. Agkaggregin has an apparent molecular mass of about 28 kDa and consists of two different types of subunits, an alpha-subunit (approximately 15 kDa) and a beta-subunit (approximately 14 kDa). Agkaggregin has the ability to induce platelet aggregation at concentrations of the order of nanomoles. The agkaggregin crystals grew for nearly a year by hanging-drop vapour diffusion and belong to the I222 space group, with unit-cell parameters a = 64.75, b = 74.21, c = 133.24 A. One asymmetric unit contains one alphabeta heterodimer, corresponding to a volume-to-mass ratio of 2.795 A(3) Da(-1). Agkaggregin may exist in two association forms: an alphabeta heterodimer and a dimer of alphabeta heterodimers that associates during the long process of crystallization.
Liu
Sijiu
S
Key Laboratory of Structural Biology, University of Science and Technology of China, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
Zhu
Zhongliang
Z
Sun
Jinpeng
J
Zhu
Zhiqiang
Z
Huang
Qingqiu
Q
Teng
Maikun
M
Niu
Liwen
L
D003435:Crotalid Venoms / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D037102:Lectins / Q000737:chemistry*; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry*
C031442:Agkistrodon venoms; D003435:Crotalid Venoms; D037102:Lectins; D010975:Platelet Aggregation Inhibitors