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
| Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
|---|---|
| Data(s) |
17/11/2015
17/11/2015
01/01/2007
|
| Resumo |
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. |
| Formato |
698-701 |
| Identificador |
http://dx.doi.org/10.2174/092986607781483796 Protein and Peptide Letters, v. 14, n. 7, p. 698-701, 2007. 0929-8665 http://hdl.handle.net/11449/130626 10.2174/092986607781483796 WOS:000253577200011 2-s2.0-34548669385 |
| Idioma(s) |
eng |
| Publicador |
Bentham Science Publ Ltd |
| Relação |
Protein and Peptide Letters |
| Direitos |
closedAccess |
| Palavras-Chave | #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 |
| Tipo |
info:eu-repo/semantics/article |
