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Preliminary X-Ray Crystallographic Studies of a Lys49-Phospholipase A2 Homologue from Bothrops pirajai Venom Complexed with p-Bromophenacyl Bromide and α-Tocopherol Inhibitors

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PrTX-I, a non-catalytic and myotoxic Lys49-PLA2 from Bothrops pirajai venom has been crystallized alone and in complex with bromophenacyl bromide (BPB), α-tocopherol and α-tocopherol acetate inhibitors. These crystals have shown to diffract X-rays between 2.34 and 1.65 Å resolution. All complexes crystals are isomorphous and belong to the space group P21 whereas native PrTX-I crystals belong to the P3121.





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Keywords: Bothrops pirajai venom; Crystallization; Lys49-phospholipase A2; X-ray crystallography; myotoxity; p-BPB; pbromophenacyl bromide; vitamin E; α-tocopherol

Document Type: Research Article

Publication date: 2007-07-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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