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Molecular dynamics simulations of phospholipases A2.
Demaret, J P; Brunie, S.
Afiliação
  • Demaret JP; Laboratoire de Biochimie (CNRS UA 240), Ecole Polytechnique, Palaiseau, France.
Protein Eng ; 4(2): 163-70, 1990 Dec.
Article em En | MEDLINE | ID: mdl-2075191
An extensive molecular dynamics study of phospholipases A2 from pancreatic bovine and Crotalus atrox venom has shown that the well-conserved homologous core of the phospholipases A2, including the so called catalytic network, is very stable during the course of the calculations. The fluctuations which occur are located in segments which have significantly different three-dimensional conformations in the two phospholipases A2 studied, suggesting that a particularly stable core conformation gives rise to a large homologous family of similar three-dimensional structure. The calcium ion, which exhibits a crucial structural role in the monomeric phospholipases A2, appears not to be required to stabilize the C.atrox dimer. Moreover, the behaviour of the dimeric structure during the dynamics raises the question of a possible dissociation of the two subunits into functional monomers.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases A / Modelos Moleculares Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: Protein Eng Assunto da revista: BIOQUIMICA / BIOTECNOLOGIA Ano de publicação: 1990 Tipo de documento: Article País de afiliação: França
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases A / Modelos Moleculares Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: Protein Eng Assunto da revista: BIOQUIMICA / BIOTECNOLOGIA Ano de publicação: 1990 Tipo de documento: Article País de afiliação: França