Molecular dynamics simulation of a phospholipase A2-substrate complex.

S T Jones; P Ahlström; H J Berendsen; R W Pickersgill

doi:10.1016/0167-4838(93)90139-i

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Molecular dynamics simulation of a phospholipase A2-substrate complex.

S T Jones·P Ahlström·H J Berendsen·R W Pickersgill

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Abstract

We have used knowledge of the three-dimensional structure of phospholipids and phospholipases A2 together with biochemical data, computer graphics modelling and a 48 ps molecular dynamics simulation to predict the structure of a phospholipase A2-substrate complex. There is remarkable similarity between this predicted structure of enzyme-substrate complex and the structure that can be deduced from the observed enzyme-inhibitor complex. Molecular dynamics simulation highlights the importance of the calcium-ion in substrate binding and the persistence of the His-48 to water-hydrogen bond is compatible with the proposed role of this water molecule as the nucleophile in catalysis.

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Animals Binding Sites Calcium Computer Simulation Models, Molecular Molecular Structure Phosphatidylcholines Phospholipases A Phospholipases A2 Substrate Specificity Swine Water Comparative Study Journal Article Research Support, Non-U.S. Gov't

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S T Jones, P Ahlström, H J Berendsen, R W Pickersgill. 1993-03-05. Molecular dynamics simulation of a phospholipase A2-substrate complex.. https://doi.org/10.1016/0167-4838(93)90139-i

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