1bp1
From Proteopedia
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'''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN''' | '''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN''' | ||
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[[Category: Carroll, S F.]] | [[Category: Carroll, S F.]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
| - | [[Category: | + | [[Category: Antibiotic]] |
| - | [[Category: | + | [[Category: Bactericidal]] |
| - | [[Category: | + | [[Category: Lipid-binding]] |
| - | [[Category: | + | [[Category: Lipopolysaccharide-binding]] |
| - | [[Category: | + | [[Category: Permeability-increasing]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:47:18 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:47, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 11:47:18 2008
