Title : Structural and dynamic characterization of the interaction of the putative fusion peptide of the S2 SARS-CoV virus protein with lipid membranes.

Pub. Date : 2008 Jun 12

PMID : 18489147






4 Functional Relationships(s)
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Protein Name
Organism
1 We demonstrate that SARS FP strongly partitions into phospholipid membranes, more specifically with those containing negatively charged phospholipids, increasing the water penetration depth and displaying membrane-activity modulated by the lipid composition of the membrane. Phospholipids seryl-tRNA synthetase 1 Homo sapiens
2 We demonstrate that SARS FP strongly partitions into phospholipid membranes, more specifically with those containing negatively charged phospholipids, increasing the water penetration depth and displaying membrane-activity modulated by the lipid composition of the membrane. Phospholipids seryl-tRNA synthetase 1 Homo sapiens
3 These data suggest that SARS FP could be involved in the merging of the viral and target cell membranes by perturbing the membrane outer leaflet phospholipids and specifically interacting with negatively charged phospholipids located in the inner leaflet. Phospholipids seryl-tRNA synthetase 1 Homo sapiens
4 These data suggest that SARS FP could be involved in the merging of the viral and target cell membranes by perturbing the membrane outer leaflet phospholipids and specifically interacting with negatively charged phospholipids located in the inner leaflet. Phospholipids seryl-tRNA synthetase 1 Homo sapiens