Mini-Symposium - Abstracts
12 AT THE INTERFACE II: MOLECULAR INTERACTIONS AMONG MYOTOXIC CALCIUM-INDEPENDENT PHOSPHOLIPASE A2 HOMOLOGUES, LIPIDS AND FATTY ACIDS
R.K. ARNI
Department of Physics, Institute of Biosciences, Humanities and Physical Sciences, São Paulo State University, São José do Rio Preto, SP, Brazil.
Phospholipases A2 (PLA2) play crucial roles in the regulation of many cellular processes such as blood platelet aggregation and acute hypersensitivity. These processes are mediated by intracellular PLA2 activity in cell membranes which release arachiodonic acid, the precursor of a diverse group of messengers including prostaglandins, leukotrines or tromboxanes. Disturbances in arachadonic acid metabolism may lead to pathophysiological responses such as rheumatoid arthritis and asthma. Thus, the understanding of PLA2 is essential in the development of therapies for these diseases. The key to developing pharmacological agents against intracellular PLA2s is dependent on a detailed knowledge of the interaction of the protein with lipid substrates at the molecular level. The crystal structures of PLA2s complexed with transition-state analogues have been determined. However, no structural information is currently available for the natural PLA2/phospholipd complexes.
We have determined the crystal structures of five monomeric and dimeric myotoxic K49 PLA2s. The focus of our structural studies is the determination of the crystal structures of catalytically inactive PLA2 homologues both in the native state and complexed with phospholipds and fatty acids.
Financial support: FAPESP and CNPq.
CORRESPONDENCE TO:
Dr. Raghuvir K. Arni - Departamento de Física, IBILCE, UNESP, Rua Cristóvão Colombo, 2265, CEP 15054-000, São José do Rio Preto, SP, Brasil. email: arni@thor.ibilce.unesp.br
Publication Dates
-
Publication in this collection
08 Jan 1999 -
Date of issue
1997
