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- Crystal structure of myotoxin II, a monomeric Lys49-Phospholipase A(2) homologue isolated from the venom of Cerrophidion (Bothrops) godmani
- Universidade Estadual Paulista (UNESP)
- Universidade de São Paulo (USP)
- Fac Associadas Sao Paola
- Univ Costa Rica
- Lys49-Phospholipase A(2) (Lys49-PLA(2)) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we have solved the crystal structure of myotoxin-II, a Lys49-PLA(2) isolated from the venom of Cerrophidion (Bothrops) godmani (godMT-II) at 2.8 Angstrom resolution by molecular replacement. The final model has been refined to a final crystallografic residual (R-factor) of 18.8% (R-free = 28.2%), with excellent stereochemistry. godMT-II is also monomeric in the crystalline state, and small-angle X-ray scattering results demonstrate that the protein is monomeric in solution under fisicochemical conditions similar to those used in the crystallographic studies. (C) 1999 Academic Press.
- Archives of Biochemistry and Biophysics. San Diego: Academic Press Inc., v. 366, n. 2, p. 177-182, 1999.
- Academic Press Inc.
- snake venoms
- Lys49-Phospholipase A(2)
- Cerrophidion (Bothrops) godmani
- Acesso restrito
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