VENOM PROTEINS AS STRUCTURAL MODEL SYSTEMS

ARNI, R. K.(1)

(1)Department of Physics, IBILCE-UNESP, São José do Rio Preto, SP, CEP 15054-000.

The action and damage caused by snake venom proteins have been extensively studied and provide us with an excellent oppurtunity to correlate structural information with pharmacological and biochemical data to improve our understanding of their function and mode of action. These proteins are involved in aa number of key biological processes such as membrane damage, lipid hydrolysis, myotoxicity, hemostasis, fibrinolysis and blood coagulation. High resolution diffraction data have been collected from a number of snake venom phospholipases both in the native states and bound to fatty acids, amphiphiles, phospholipids and inhibitors. This provides us with a wealth of information about the mode of action and stereochemical requirements of these enzymes. Structural data is also available for a number of snake venom thrombin-like enzymes currently being studied in our laboratory and structural comparisons with the serine proteases involved in the control and regulation of blood coagulation should be important for the design of novel inhibitors and substrates. This presentation will focus on the structural aspects of these important venom proteins.

Acknowledgements: Financial support  by FAPESP and CNPq is gratefully acknowledged.

CORRESPONDENCE TO:

ARNI, R. K., Department of Physics, IBILCE-UNESP, São José do Rio Preto, SP, CEP 15054-000, Brasil, Email: arni@df.ibilce.unesp.br