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Gewählte Publikation:

Grandits, M; Oostenbrink, C.
(2015): Selectivity of cytosolic phospholipase A2 type IV toward arachidonyl phospholipids
J MOL RECOGNIT. 2015; 28(7): 447-457. FullText FullText_BOKU

Cytosolic phospholipase A2 (cPLA(2)) is an interesting protein involved in inflammatory processes and various diseases. Its catalytic mechanism as well as its substrate specificity for arachidonyl phospholipids is not typical for other phospolipases. Furthermore, a lid structure, which ensures a hydrophilic surface of the protein without any substrate bound and the movement of this flexible loop to make the hydrophobic active site accessible, is of high interest. Therefore, the focus of this work was to determine the binding mode of cPLA(2) with various substrates, such as arachidonic acid, a synthetic inhibitor, a saturated phospholipid, and most importantly an arachidonyl phospholipid. To understand the selectivity of the protein toward the arachidonyl phospholipid and the interaction in a protein-ligand complex, molecular dynamics simulations were performed using the GROMOS suite of simulation programs. The simulations provide insight into the protein and showed that selective binding of arachidonyl phospholipids is because of the shape of the sn-2 tail. The amino acids Asn555 and Ala578 are involved in the strongest interactions observed in the protein-ligand complexes. Copyright (c) 2015 John Wiley *** Sons, Ltd.
Autor*innen der BOKU Wien:
Grandits Melanie
Oostenbrink Chris

Find related publications in this database (Keywords)
cytosolic phospholipase A2 type IV
alpha/beta hydrolase
arachidonyl phospholipid
arachidonic acid
molecular dynamics simulations

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