Molecular dynamics simulations of phospholipases A2

• Published in: Protein engineering 1990-12, Vol.4 (2), p.163-170
• Main Authors: Demaret, Jean-Philippe, Brunie, Simone
• Format: Article
• Language: English
• Subjects: Animals; Biological and medical sciences; Biotechnology; Calcium - metabolism; Cattle; Crotalid Venoms; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Models, Molecular; molecular dynamics simulations; molecular mechanics; Pancreas - enzymology; phospholipase A2; Phospholipases A - chemistry; Phospholipases A - metabolism; Protein Conformation; Protein engineering; Sequence Homology, Nucleic Acid; Thermodynamics; X-Ray Diffraction
• ISSN: 1741-0126; 0269-2139; 1741-0134; 1460-213X
• DOI: 10.1093/protein/4.2.163

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.