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Protein Engineering vol. 4 no. 2 pp. 171-176, 1990
© 1990 Oxford University Press

RESEARCH-ARTICLE

Dimeric character of a basic phospholipase A2 from cobra venom: experimental and modelling study

Jean-Philippe Demaret, Serg Chwetzoff1 and Simone Brunie2

Laboratoire de Biochimie (CNRS UA 240). Ecole Polytechnique 91128 Palaiseau Cedex, France 1Centre de Recherche de I'INRA labaratoire de Virologie et d'Immunologie Moléculaires 78350 Jouyen-Josas, France

2To whom correspondence should be addressed

When it is gel filtered on Sephadex in the absence of calcium ions, basic phospholipase A2 from Naja nigricollis venom elutes as a dimer. In order to study the possibility of this dimerization from a structural point of view, three-dimensional models of both monomeric and dimeric N. nigricollis phospholipases A have been graphically built on the basis of homologies with the phospholipases A2 from pancreatic bovine and Crotalus atrox venom. The building of a duneric model is made possible by the deletion of a particular loop of the bovine structure. The predicted models of N. nigricollis phospholipase A2 have been checked using molecular mechanics and molecular dynamics techniques according to a suitable protocol which has been developed starting from refined X-ray structures of phospholipases A2 as the test case. The observed stability of the dimeric model, in the absence of calcium, agrees with the hypothesis of the dimerization of the basic phospholipase A Particularly, Arg31, which replaces the hydrophobic residue present in pancreatic bovine and C.atrox venom phospholipases A2, contributes to this stability.

Keywords: homology modelling/model building/molecular dynamics stimulations/molecular mechanics/phospholipase A2

Received April 24, 1990; accepted September 26, 1990.


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