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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5320
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pubmed:dateCreated |
1997-7-1
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1861-4
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9188532-Amino Acid Sequence,
pubmed-meshheading:9188532-Antimicrobial Cationic Peptides,
pubmed-meshheading:9188532-Binding Sites,
pubmed-meshheading:9188532-Blood Bactericidal Activity,
pubmed-meshheading:9188532-Blood Proteins,
pubmed-meshheading:9188532-Crystallization,
pubmed-meshheading:9188532-Crystallography, X-Ray,
pubmed-meshheading:9188532-Humans,
pubmed-meshheading:9188532-Lipopolysaccharides,
pubmed-meshheading:9188532-Membrane Proteins,
pubmed-meshheading:9188532-Models, Molecular,
pubmed-meshheading:9188532-Molecular Sequence Data,
pubmed-meshheading:9188532-Phosphatidylcholines,
pubmed-meshheading:9188532-Protein Conformation,
pubmed-meshheading:9188532-Protein Structure, Secondary,
pubmed-meshheading:9188532-Protein Structure, Tertiary
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pubmed:year |
1997
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pubmed:articleTitle |
Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.
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pubmed:affiliation |
UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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