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Open AccessOpen Access JUSTC Original Paper

Structural biology of some snake venom protein families

  • School of Life Science, University of Science and Technology of China, Hefei 230027, China

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  • Corresponding author: NIU Li-wen, E-mail: lwniu@ustc.edu.cn
  • Received Date: 05 July 2008
  • Rev Recd Date: 10 August 2008
  • Publish Date: 31 August 2008
    Abstract

  • Abstract

    Following the clues from our groups characteristic investigations of five snake venom protein families, a short review was provided on some research conclusions, current opinions and latest advances from structural biology of snake venom protein families of serine proteases, metalloproteinase, CRISP, phospholipase A2 and neurotoxin as well. This review emphasized the importance of structural biology of snake venom glycoproteins, crystal structures at an ultrahigh resolution and the complex structure related to snake venom proteins in the field of snake venom proteins.

    Abstract

    Following the clues from our groups characteristic investigations of five snake venom protein families, a short review was provided on some research conclusions, current opinions and latest advances from structural biology of snake venom protein families of serine proteases, metalloproteinase, CRISP, phospholipase A2 and neurotoxin as well. This review emphasized the importance of structural biology of snake venom glycoproteins, crystal structures at an ultrahigh resolution and the complex structure related to snake venom proteins in the field of snake venom proteins.
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    • References(85)
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    [1]
    Fox J W, Serrano S M. Exploring snake venom proteomes: multifaceted analyses for complex toxin mixtures[J]. Proteomics, 2008,8(4): 909-920.
    [2]
    Pahari S, Mackessy S P, Kini R M. The venom gland transcriptome of the Desert Massasauga rattlesnake (Sistrurus catenatus edwardsii): towards an understanding of venom composition among advanced snakes (Superfamily Colubroidea)[J]. BMC Mol Biol, 2007,8: 115.
    [3]
    Moura-da-Silva A M, Butera D, Tanjoni I. Importance of snake venom metalloproteinases in cell biology: effects on platelets, inflammatory and endothelial cells[J]. Curr Pharm Des, 2007,13(28): 2 893-2 905.
    [4]
    Bjarnason J B, Fox J W. Hemorrhagic metalloproteinases from snake venoms[J]. Pharmacol Ther, 1994,62(3): 325-372.
    [5]
    Fox J W, Serrano S M. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases[J]. Toxicon, 2005,45(8): 969-985.
    [6]
    Gomis-Ruth F X, Kress L F, Kellermann J, et al. Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin[J]. J Mol Biol, 1994,239(4): 513-544.
    [7]
    Zhang D, Botos I, Gomis-Rueth F X, et al. Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)[J]. Proc Natl Acad Sci U S A, 1994,91(18): 8 447-8 451.
    [8]
    Kumasaka T, Yamamoto M, Moriyama H, et al. Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis[J]. J Biochem, 1996,119(1): 49-57.
    [9]
    Zhu X, Teng M, Niu L. Structure of acutolysin-C, a haemorrhagic toxin from the venom of Agkistrodon acutus, providing further evidence for the mechanism of the pH-dependent proteolytic reaction of zinc metalloproteinases[J]. Acta Crystallogr D Biol Crystallogr, 1999,55(Pt 11): 1 834-1 841.
    [10]
    Huang K F, Chiou S H, Ko T P, et al. The 1.35 A structure of cadmium-substituted TM-3, a snake-venom metalloproteinase from Taiwan habu: elucidation of a TNFalpha-converting enzyme-like active-site structure with a distorted octahedral geometry of cadmium[J]. Acta Crystallogr D Biol Crystallogr, 2002,58(Pt 7): 1 118-1 128.
    [11]
    Watanabe L, Shannon J D, Valente R H, et al. Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities[J]. Protein Sci, 2003,12(10): 2 273-2 281.
    [12]
    Lou Z, Hou J, Liang X, et al. Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus[J]. J Struct Biol, 2005,152(3): 195-203.
    [13]
    Bode W, Gomis-Ruth F X, Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’[J]. FEBS Lett, 1993,331(1-2): 134-140.
    [14]
    Gong W, Zhu X, Liu S, et al. Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus[J]. J Mol Biol, 1998,283(3): 657-668.
    [15]
    Takeda S, Igarashi T, Mori H, et al. Crystal structures of VAP1 reveal ADAMs MDC domain architecture and its unique C-shaped scaffold[J]. EMBO J, 2006,25(11): 2 388-2 396.
    [16]
    Igarashi T, Araki S, Mori H, et al. Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins[J]. FEBS Lett, 2007,581(13): 2 416-2 422.
    [17]
    Takeda S, Igarashi T, Mori H. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases[J]. FEBS Lett, 2007,581(30): 5 859-5 864.
    [18]
    Zang J, Zhu Z, Yu Y, et al. Purification, partial characterization and crystallization of acucetin, a protein containing both disintegrin-like and cysteine-rich domains released by auto-proteolysis of a P-III-type metalloproteinase AaH-IV from Agkistrodon acutus venom[J]. Acta Crystallogr D Biol Crystallogr, 2003,59(Pt 12): 2 310-2 312.
    [19]
    Braud S, Bon C, Wisner A. Snake venom proteins acting on hemostasis[J]. Biochimie, 2000,82(9-10): 851-859.
    [20]
    Matsui T, Fujimura Y, Titani K. Snake venom proteases affecting hemostasis and thrombosis[J]. Biochim Biophys Acta, 2000,1477(1-2): 146-156.
    [21]
    Parry M A, Jacob U, Huber R, et al. The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases[J]. Structure, 1998,6(9): 1 195-1 206.
    [22]
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