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

Santos, Juliana I. dos [UNESP]Marchi-Salvador, Daniela P. [UNESP]Fernandes, Carlos A. H. [UNESP]Silveira, Lucas B.Soares, Andreimar M.Fontes, Marcos R. M. [UNESP]2015-11-172015-11-172007-01-01Protein and Peptide Letters, v. 14, n. 7, p. 698-701, 2007.0929-8665http://hdl.handle.net/11449/130626PrTX-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)21.698-701engα-tocopherolBothrops pirajai venomCrystallizationLys49-phospholipase A2Myotoxityp-BPBP-bromophenacyl bromideVitamin EX-ray crystallographyAlpha tocopherolBromideEnzyme inhibitorLysinePhospholipase ASnake venomAnimalChemical structureChemistryProtein conformationSnakeX ray crystallographyAlpha-TocopherolAnimalsBothropsBromidesCrotalid VenomsCrystallography, X-RayEnzyme InhibitorsLysineModels, MolecularPhospholipases AProtein ConformationBothrops pirajaiPreliminary X-ray crystallographic studies of a Lys49-phospholipase A(2) homologue from Bothrops pirajai venom complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitorsArtigo10.2174/092986607781483796WOS:000253577200011Acesso restrito2-s2.0-34548669385