Back to Search
Start Over
Crystallization and preliminary X-ray diffraction studies of BmooPLA2-I, a platelet-aggregation inhibitor and hypotensive phospholipase A2 from Bothrops moojeni venom.
- Source :
- Acta Crystallographica: Section F (Wiley-Blackwell); Aug2011, Vol. 67 Issue 8, p900-902, 3p
- Publication Year :
- 2011
-
Abstract
- Phospholipases A<subscript>2</subscript> (PLA<subscript>2</subscript>s) are enzymes that cause the liberation of fatty acids and lysophospholipids by the hydrolysis of membrane phospholipids. In addition to their catalytic action, a wide variety of pharmacological activities have been described for snake-venom PLA<subscript>2</subscript>s. BmooPLA<subscript>2</subscript>-I is an acidic, nontoxic and catalytic PLA<subscript>2</subscript> isolated from Bothrops moojeni snake venom which exhibits an inhibitory effect on platelet aggregation, an immediate decrease in blood pressure, inducing oedema at a low concentration, and an effective bactericidal effect. BmooPLA<subscript>2</subscript>-I has been crystallized and X-ray diffraction data have been collected to 1.6 Å resolution using a synchrotron-radiation source. The crystals belonged to space group C222<subscript>1</subscript>, with unit-cell parameters a = 39.7, b = 53.2, c = 89.2 Å. The molecular-replacement solution of BmooPLA<subscript>2</subscript>-I indicated a monomeric conformation, which is in agreement with nondenaturing electrophoresis and dynamic light-scattering experiments. A comparative study of this enzyme with the acidic PLA<subscript>2</subscript> from B. jararacussu (BthA-I) and other toxic and nontoxic PLA<subscript>2</subscript>s may provide important insights into the functional aspects of this class of proteins. [ABSTRACT FROM AUTHOR]
- Subjects :
- PHOSPHOLIPASE A2
BOTHROPS
LYSOPHOSPHOLIPIDS
CRYSTALLIZATION
X-ray diffraction
Subjects
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 67
- Issue :
- 8
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 110812835
- Full Text :
- https://doi.org/10.1107/S174430911102392X