Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution
摘要：
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.
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关键词：
Humans Blood Proteins Phosphatidylcholines Membrane Proteins Crystallography, X-Ray Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Binding Sites Amino Acid Sequence
DOI：
10.1126/science.276.5320.1861
被引量：
年份：
1997
Wiley
掌桥科研
Semantic Scholar
万方医学
NCBI
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