1bp1
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(New page: 200px<br /> <applet load="1bp1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bp1, resolution 2.40Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:29, 29 October 2007
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CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN
Overview
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.
About this Structure
1BP1 is a [Single protein] structure of sequence from [Homo sapiens] with PC1 as [ligand]. Full crystallographic information is available from [OCA].
Reference
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
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