1BP1
CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN
Summary for 1BP1
| Entry DOI | 10.2210/pdb1bp1/pdb |
| Descriptor | BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN, 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total) |
| Functional Keywords | bactericidal, permeability-increasing, lipid-binding, lipopolysaccharide-binding, antibiotic |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 52283.98 |
| Authors | Beamer, L.J.,Carroll, S.F.,Eisenberg, D. (deposition date: 1997-04-08, release date: 1997-09-04, Last modification date: 2024-11-06) |
| Primary citation | Beamer, L.J.,Carroll, S.F.,Eisenberg, D. Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science, 276:1861-1864, 1997 Cited by PubMed Abstract: 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. PubMed: 9188532DOI: 10.1126/science.276.5320.1861 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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