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http://acervodigital.unesp.br/handle/11449/130626- Title:
- Preliminary X-ray crystallographic studies of a Lys49-phospholipase A(2) homologue from Bothrops pirajai venom complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors
- 0929-8665
- PrTX-I, a non-catalytic and myotoxic Lys49-PLA(2) from Bothrops pirajai venom has been crystallized alone and in complex with bromophenacyl bromide (BPB), alpha-tocopherol and alpha-tocopherol acetate inhibitors. These crystals have shown to diffract X-rays between 2.34 and 1.65 angstrom resolution. All complexes crystals are isomorphous and belong to the space group P2(1) whereas native PrTX-I crystals belong to the P3(1)21.
- 1-Jan-2007
- Protein and Peptide Letters, v. 14, n. 7, p. 698-701, 2007.
- 698-701
- Bentham Science Publ Ltd
- α-tocopherol
- Bothrops pirajai venom
- Crystallization
- Lys49-phospholipase A2
- Myotoxity
- p-BPB
- P-bromophenacyl bromide
- Vitamin E
- X-ray crystallography
- Alpha tocopherol
- Bromide
- Enzyme inhibitor
- Lysine
- Phospholipase A
- Snake venom
- Animal
- Chemical structure
- Chemistry
- Protein conformation
- Snake
- X ray crystallography
- Alpha-Tocopherol
- Animals
- Bothrops
- Bromides
- Crotalid Venoms
- Crystallography, X-Ray
- Enzyme Inhibitors
- Lysine
- Models, Molecular
- Phospholipases A
- Protein Conformation
- Bothrops pirajai
- http://dx.doi.org/10.2174/092986607781483796
- Acesso restrito
- outro
- http://repositorio.unesp.br/handle/11449/130626
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