Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.
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Beamer LJ, Carroll SF, Eisenberg D
Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.
Science. 1997 Jun 20;276(5320):1861-4.
- PubMed ID
- 9188532 [ View in PubMed]
- Abstract
Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.