Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.,Beamer LJ, Carroll SF, Eisenberg D Science. 1997 Jun 20;276(5320):1861-4. PMID:9188532[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. PMID:9188532
