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