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dc.contributor.author한경림-
dc.contributor.authorRichard W. Pastor-
dc.contributor.authorCristina Fenollar-ferrer-
dc.date.accessioned2021-06-09T04:26:22Z-
dc.date.available2021-06-09T04:26:22Z-
dc.date.issued2020-07-
dc.identifier.citationVOL 15, NO 7, e0236201-
dc.identifier.issn1932-6203-
dc.identifier.other56794-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/73085-
dc.description.abstractInteraction of phospholipase D2 (PLD2) with phosphatidylinositol (4,5)-bisphosphate (PIP2) is regarded as the critical step of numerous physiological processes. Here we build a full-length model of human PLD2 (hPLD2) combining template-based and ab initio modeling techniques and use microsecond all-atom molecular dynamics (MD) simulations of the protein in contact with a complex membrane to determine hPLD2-PIP2 interactions. MD simulations reveal that the intermolecular interactions preferentially occur between specific PIP2 phosphate groups and hPLD2 residues-
dc.description.abstractthe most strongly interacting residues are arginine at the pbox consensus sequence (PX) and pleckstrin homology (PH) domain. Interaction networks indicate formation of clusters at the protein-membrane interface consisting of amino acids, PIP2, and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidic acid (POPA)-
dc.description.abstractthe largest cluster was in the PH domain.-
dc.publisherPLoS ONE-
dc.titlePLD2-PI(4,5)P2 Interactions in Fluid Phase Membranes: Structural Modeling and Molecular Dynamics Simulations-
dc.typeArticle-
dc.relation.pagee0236201-
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