Title : Mechanism of membrane binding of the phospholipase D1 PX domain.

Pub. Date : 2004 Dec 24

PMID : 15475361






3 Functional Relationships(s)
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1 Consistent with the model structure that suggests the presence of a second lipid-binding pocket, vesicle binding studies indicated that the PLD1 PX domain could also bind with moderate affinity to PA, phosphatidylserine, and other anionic lipids, which were mediated by a cluster of cationic residues in the secondary binding site. Phosphatidic Acids phospholipase D1 Homo sapiens
2 Collectively, our results suggest that the interaction of the PLD1 PX domain with PtdIns(3,4,5)P(3) and/or PA (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1. Phosphatidic Acids phospholipase D1 Homo sapiens
3 Collectively, our results suggest that the interaction of the PLD1 PX domain with PtdIns(3,4,5)P(3) and/or PA (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1. Phosphatidic Acids phospholipase D1 Homo sapiens