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Oral 39. Congresso da Sociedade Brasileira de Toxinologia, 8., Symposium of the Pan American Section of the International Society on Toxinology, 8., 2004, Angra dos Reis, Brasil. Abstracts... J. Venom. Anim. Toxins incl.Trop. Dis., 2004, 10, 3, p.357. |
Structural Aspects Underlying The Multi-funcionality Of Venom Proteins.
Departamento de Física, IBILCE/UNESP, São Jose do Rio Preto, São Paulo.
Proteins abound with sites for binding and recognition of other proteins, lipids, ions, solvent and small molecules to enable them to carry out their functions. Amino acid sequence changes lead to modifications of the surface charges, specificity and mode of action. Snake venom proteins are structurally highly homologous to mammalian proteins and utilize the same basic structural motif. However, their aim is to disrupt and interfere in a wide spectrum of essential physiological functions. These differences that arise from minor modifications without significant change in the motifs have been analyzed based on the atomic resolution structures of venom D49/K49 PLA2s, metalloproteases and C-type lectins. Structural models which attempt to delineate and account for anticoagulant, haemolytic, inhibition of platelet aggregation and myotoxicity will be presented.
Acknowledgements: Financial support by FAPESP and CNPq is gratefully acknowledged.