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Science 20 June 1997:
Vol. 276. no. 5320, pp. 1861 - 1864
DOI: 10.1126/science.276.5320.1861

Reports

Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution

Lesa J. Beamer, Stephen F. Carroll, David Eisenberg *

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.

L. J. Beamer and D. Eisenberg, UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.
S. F. Carroll, XOMA Corporation, 2910 Seventh Street, Berkeley, CA 94710, USA.
*   To whom correspondence should be addressed.


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